Outer membrane protein of Ehrlichia canis and Ehrlichia chaffeensis

ABSTRACT

Diagnostic tools for for serodiagnosing ehrlichiosis in mammals, particularly in members of the Canidae family and in humans are provided. The diagnostic tools are a group of outer membrane proteins of  E. chaffeensis  and variants thereof, referred to hereinafter as the “OMP proteins”, a group of outer membrane proteins of  E. canis  and variants thereof referred to hereinafter as the “P30F proteins”, and antibodies to the OMP proteins and the P30F proteins. The OMP proteins of  E. chaffeensis  encompass OMP-1, OMP-1A, OMP1-B, OMP-1C, OMP1-D, OMP1-E, OMP1-F, OMP1-H, OMP-1R, OMP-1S, OMP-1T, OMP-1U, OMP-1V, OMP-1W, OMP-1X, OMP-1Y and OMP-1Z. The P30F proteins of  E. canis  encompass P30, P30 a,  P30-1, P30-2, P30-3, P30-4, P30-5, P30-6, P30-7, P30-8, P30-9, P30-10, P30-11, and P30-12. Isolated polynucleotides that encode the  E. chaffeensis  OMP proteins and isolated polynucleotides that encode the  E. canis  P30F protein are also provided. The present invention also relates to kits containing reagents for diagnosing human ehrlichiosis and canine ehrlichiosis, and to immunogenic compositions containing one or more OMP proteins or P30F proteins.

[0001] This work was supported by grant RO1 AI33123 and RO1 AI40934 from National Institutes of Health. The government has certain rights in this invention.

BACKGROUND OF THE INVENTION

[0002] The ehrlichiae are obligate intracellular bacteria that infect circulating leucocytes. Ehrlichia chaffeensis infects the monocytes and macrophages in humans and causes human monocytic ehrlichiosis. The clinical manifestations of ehrlichiosis in humans are nonspecific and similar to Rocky Mountain spotted fever. The clinical manifestations include fever, chills, headache, myalgia or vomiting, and weight loss. Most patients have a history of tick exposure.

[0003]Ehrlichia canis infects and causes ehrlichiosis in animals belonging to the family Canidae. Canine ehrlichiosis consists of an acute and a chronic phase. The acute phase is characterized by fever, serous nasal and ocular discharges, anorexia, depression, and loss of weight. The chronic phase is characterized by severe pancytopenia, epistaxis, hematuria, blood in feces in addition to more severe clinical signs of the acute disease. If treated early during the course of the disease, dogs respond well to doxycycline. However, chronically infected dogs do not, respond well to the antibiotic. Therefore, early diagnosis is very important for treating canine ehrlichiosis.

[0004] The primary diagnostic test for diagnosing canine ehrlichiosis and human ehrlichiosis is the indirect fluorescent antibody (IFA) test. This test uses the etiologic agent Ehrlichia canis to diagnose canine ehrlichiosis. The IFA test uses Ehrlichia chaffeensis as antigen for diagnosing human ehrlichiosis. The IFA test has, however, serious limitations. The IFA test is subject to false positives because the antigens are made of whole infected cells which comprise many nonspecific proteins which will cross-react with sera from some patients. The IFA test is also subject to false negatives because IFA antigens are unstable and may become inactivated during storage. In addition the IFA test requires a special equipment to perform the test. For example, the IFA test requires a tissue culture system for growing the bacterium that are used to prepare the antigen slides, a fluorescent microscope, and trained persons to evaluate the serum reactivity to the bacterial antigen on the slide.

[0005] Tools which permit simpler, more rapid, and objective serodiagnosis of canine ehrlichiosis or human ehrlichiosis are desirable.

SUMMARY OF THE INVENTION

[0006] The present invention relates to improved diagnostic tools for veterinary and human use which are used for serodiagnosing ehrlichiosis in mammals, particularly in members of the Canidae family and in humans. The diagnostic tools are a group of outer membrane proteins of E. chaffeensis and variants thereof, referred to hereinafter as the “OMP proteins”, a group of outer membrane proteins of E. canis and variants thereof referred to hereinafter as the “P30F proteins”, and antibodies to the OMP proteins and the P30F proteins.

[0007] The OMP proteins of E. chaffeensis encompass OMP-1, OMP-1A, OMP1-B, OMP-1C, OMP1-D, OMP1-E, OMP1-F, OMP1-H, OMP-1R, OMP-1S, OMP-1T, OMP-1U, OMP-1V, OMP-1W, OMP-1X, OMP-1Y and OMP-1Z. The mature OMP-1 protein of E. chaffeensis has a molecular weight of about 27.7 kDa and comprises amino acid 26 through amino acid 281 of the sequence shown in FIG. 3B, SEQ ID NO: 2. The mature OMP-1B protein of E. chaffeensis has a molecular weight of about 28.2 kDa and comprises amino acid 26 through amino acid 283 of the sequence shown in FIG. 4B, SEQ ID NO: 4. The mature OMP-1C protein of E. chaffeensis has a molecular weight of about 27.6 kDa and comprises amino acid 26 through amino acid 280 of the sequence shown in FIG. 5B, SEQ ID NO: 6. The mature OMP-1D protein of E. chaffeensis has a molecular weight of about 28.7 and comprises amino acid 26 through amino acid 286 of the sequence shown in FIG. 6B, SEQ ID NO: 8. The mature OMP-1E protein of E. chaffeensis has a molecular weight of about 27.8 kDa and comprises amino acid 26 through amino acid 278 of the sequence shown in FIG. 7B, SEQ ID NO: 10. The mature OMP-1F protein of E. chaffeensis has a molecular weight of about 27.9 kDa and comprises amino acid 26 through amino acid 280 of the sequence shown in FIG. 8B, SEQ ID NO: 12. The mature OMP-1A protein of E. chaffeensis has a molecular weight of about 29.6 kDa and comprises amino acid 31 through amino acid 297 of the sequence shown in FIG. 9B, SEQ ID NO: 14. The mature OMP-1R protein of E. chaffeensis has a molecular weight of about 19.7 kDa and comprises amino acid 29 through amino acid 196 of the sequence shown in FIG. 10B, SEQ ID NO: 16. The mature OMP-1S protein of E. chaffeensis has a molecular weight of about 29.2 kDa and comprises amino acid 26 through amino acid 291 of the sequence shown in FIG. 11B, SEQ ID NO: 18. The OMP-1T protein of E. chaffeensis comprises the amino acid sequence shown in FIG. 12B, SEQ ID NO: 20. The mature OMP-1U protein of E. chaffeensis has a molecular weight of about 30.6 kDa and comprises amino acid 26 through amino acid 295 of the sequence shown in FIG. 13B, SEQ ID NO: 22. The mature OMP-1V protein of E. chaffeensis has a molecular weight of about 28.0 kD and comprises amino acid 27 through amino acid 279 shown in FIG. 14B, SEQ ID NO: 24. The mature OMP-1W protein of E. chaffeensis has a molecular weight of about 28.8 kDa and comprises amino acid 30 through amino acid 283 of the sequence shown in FIG. 15B, SEQ ID NO: 26. The mature OMP-1X protein of E. chaffeensis has a molecular weight of about 27.8 kDa and comprises amino acid 25 through amino acid 275 of the sequence shown in FIG. 16B, SEQ ID NO: 28. The mature OMP-1Y protein of E. chaffeensis has a molecular weight about 28.8 kDa and comprises amino acid 28 through amino acid 285 of the sequence shown in FIG. 17B, SEQ ID NO: 30. The mature OMP-1Z protein of E. chaffeensis has a molecular weight of about 30.2 kDa and comprises amino acid 27 through amino acid 300 of the sequence shown in FIG. 18B, SEQ ID NO: 50. The mature OMP-1H protein has a molecular weight of about 30.2 kDa and comprises the amino acid 27 through amino acid 298 of sequence shown in FIG. 33B, SEQ ID NO: 52.

[0008] The outer membrane proteins from E. chaffeensis , particularly a recombinant form of OMP-1, are immunogenic and, thus are useful for preparing antibodies. Such antibodies are useful for immunolabeling isolates of E. chaffeensis and for detecting the presence of E. chaffeensis in body fluids, tissues, and particularly in monocytes and macrophages. The OMP proteins, particularly OMP-1, are also useful for detecting antibodies to E. chaffeensis in the blood of patients with clinical signs of ehrlichiosis. The OMP protein, particularly OMP-1, are also useful immunogens for raising antibodies that are capable of reducing the level of infection in an immunized mammal that has been infected with E. chaffeensis. The proteins are also useful in a vaccine for protecting against infection with E. chaffeensis.

[0009] The P30F proteins of E. canis encompass P30, P30a, P30-1, P30-2, P30-3, P30-4, P30-5, P30-6, P30-7, P30-8, P30-9, P30-10, P30-11, and P30-12. The mature P30 protein of E. canis has a molecular weight of about 28.8 kDa and comprises amino acid 26 through amino acid 288 of the sequence shown in FIG. 19B, SEQ ID NO: 32. The mature P30a protein of E. canis has a molecular weight of about 29.0 kDa and comprises amino acid 26 through amino acid 287 of the sequence shown in FIG. 20B, SEQ ID NO: 34. The mature P30-1 protein of E. canis has a molecular weight of about 27.7 kDa and comprises amino acid 55 through amino acid 307 of the sequence shown in FIG. 21B, SEQ ID NO: 36. The mature P30-2 protein of E. canis has a molecular weight of about 28.0 kDa and comprises amino acid 26 through amino acid 280 of the sequence shown in FIG. 22B, SEQ ID NO: 38. The mature P30-3 protein of E. canis has a molecular weight of about 28.7 kDa and comprises amino acid 26 through amino acid 283 of the sequence shown in FIG. 23B, SEQ ID NO: 40. The mature P30-4 protein of E. canis has a molecular weight of about 28.0 kDa and comprises amino acid 26 through amino acid 276 of the sequence shown in FIG. 24B, SEQ ID NO: 42. The mature P30-5 protein of E. canis has a molecular weight of about 29.4 kDa and comprises amino acid 27 through amino acid 293 of the sequence shown in FIG. 25B, SEQ ID NO: 44. The mature P30-6 protein of E. canis has a molecular weight of about 29.4 kDa and comprises amino acid 31 through amino acid 293 of the sequence shown in FIG. 26B, SEQ ID NO: 54. The mature P30-7 protein of E. canis has a molecular weight of about 29.9 kDa and comprises amino acid 31 through amino acid 296 of the sequence shown in FIG. 27B, SEQ ID NO: 56. The mature P30-8 protein of E. canis has a molecular weight of about 30.3 kDa and comprises amino acid 27 through amino acid 299 of the sequence shown in FIG. 28B, SEQ ID NO: 46. The mature P30-9 protein of E. canis has a molecular weight of about 28.6 kDa and comprises amino acid 27 through amino acid 281 of the sequence shown in FIG. 29B, SEQ ID NO: 58. The mature P30-10 protein of E. canis has a molecular weight of about 28.1 kDa and comprises amino acid 26 through amino acid 280 of the sequence shown in FIG. 30B, SEQ ID NO: 48. The mature P30-11 protein of E. canis has a molecular weight of about 28.6 kDa and comprises the amino acid 26 through amino acid 279 of sequence shown in FIG. 31B, SEQ ID NO: 60. The P30-12 protein of E. canis has a molecular weight of at least 27.3 kDa and comprises the amino acid sequence shown in FIG. 32B, SEQ ID NO: 62.

[0010] The P30F proteins, particularly P30, are immunogenic and are, thus, useful for preparing antibodies that are useful for immunolabeling isolates of E. canis. The P30 protein is also useful for diagnosing canine ehrlichiosis in mammals, particularly in members of the family Canidae, most particularly in dogs and for diagnosing infections with E. chaffeensis in humans. The P30F proteins are also useful immunogens for raising antibodies that reduce the level of infection in an immunized mammal that has been infected with E. canis. The P30F protein are also useful in a vaccine for protecting animals against infection with E. canis.

[0011] The present invention also provides isolated polynucleotides that encode the E. chaffeensis OMP proteins and isolated polynucleotides that encode the E. canis P30F proteins. The present invention also relates to antibodies which are immunospecific for and bind to the OMP proteins and the P30F proteins. Such antibodies are useful for immunolabeling isolates of E. chaffeensis and E. canis. The present invention also relates to kits containing reagents for diagnosing human ehrlichiosis and canine ehrlichiosis and to immunogenic compositions containing one or more OMP proteins or P30F proteins.

BRIEF DESCRIPTION OF THE FIGURES

[0012]FIG. 1. shows the DNA sequence and the amino acid sequence encoded by the E. chaffeensis (p28) gene cloned in pCRIIp28. The N-terminal amino acid sequence of native OMP-1 protein (P28) determined chemically is underlined. Five amino acid residues at the N terminus of P28 which were not included in the p28 gene, are indicated by boldface. Arrows indicate annealing positions of the primer pair designed for PCR.

[0013]FIG. 2. shows the restriction map of 6.3-kb genomic DNA including the omp-1 gene copies in E. chaffeensis. The four DNA fragments were cloned from the genomic DNA (pPS2.6, pPS3.6, pEC2.6, and pEC3.6). A recombinant plasmid pPS2.6 has an overlapping sequence with that of pEC3.6. The closed boxes at the bottom show PCR-amplified fragments from the genomic DNA for confirmation of the overlapping area. Open boxes at the top indicate open reading frames (ORF) of omp-1gene copies with direction by arrows. Open boxes at the bottom show DNA fragments subcloned for DNA sequencing.

[0014]FIG. 3B shows one embodiment of the OMP-1 protein; FIG. 3A shows one embodiment of the OMP-1polynucleotide.

[0015]FIG. 4B shows one embodiment of the OMP-1B protein, FIG. 4A shows one embodiment of the OMP-1B polynucleotide

[0016]FIG. 5A shows one embodiment of the OMP-1C polynucleotide; FIG. 5B shows one embodiment of the OMP-1C protein.

[0017]FIG. 6B shows one embodiment of the OMP-1D protein; FIG. 6A shows one embodiment of the OMP-1D polynucleotide.

[0018]FIG. 7B shows one embodiment of the OMP-1E protein; FIG. 7A shows one embodiment of the OMP-1E polynucleotide.

[0019]FIG. 8B shows one embodiment of the OMP-1F protein; FIG. 8A shows one embodiment of the OMP-1F polynucleotide.

[0020]FIG. 9B shows one embodiment of the OMP-1A protein, FIG. 9A shows one embodiment of the OMP-1A polynucleotide.

[0021]FIG. 10B shows one embodiment of a portion of the OMP-1R protein, FIG. 10A shows one embodiment of an OMP-1R polynucleotide encoding such polypeptide.

[0022]FIG. 11B shows one embodiment of a portion of the OMP-1S protein, FIG 11A shows one embodiment of the OMP-1S polynucleotide encoding such polypeptide.

[0023]FIG. 12B shows one embodiment of a portion of the OMP-1T protein, FIG. 12A shows one embodiment of the OMP-1T polynucleotide encoding such polypeptide.

[0024]FIG. 13B shows one embodiment of the OMP-1U protein, FIG. 13A shows one embodiment of the OMP-1U polynucleotide.

[0025]FIG. 14B shows one embodiment of the OMP-1V protein, FIG. 14A shows one embodiment of the OMP-1V polynucleotide.

[0026]FIG. 15B shows one embodiment of the OMP-1W protein, FIG. 15A shows one embodiment of the OMP-1W polynucleotide.

[0027]FIG. 16B shows one embodiment of the OMP-1X protein, FIG. 16A shows one embodiment of the OMP-1X polynucleotide.

[0028]FIG. 17B shows one embodiment of the OMP-1Y protein, FIG. 17A shows one embodiment of the OMP-1Y polynucleotide.

[0029]FIG. 18B shows one embodiment of the OMP-1Z protein, FIG. 18A shows one embodiment of the OMP-1Z polynucleotide.

[0030]FIG. 19B shows one embodiment of the P30 protein, FIG. 19A shows one embodiment of the P30 polynucleotide.

[0031]FIG. 20B shows one embodiment of the P30a protein, FIG. 20A shows one embodiment of the p30a polynucleotide.

[0032]FIG. 21B shows one embodiment of the P30-1 protein, FIG. 21A shows one embodiment of the p30-1 polynucleotide.

[0033]FIG. 22B shows one embodiment of the P30-2 protein, FIG. 22A shows one embodiment of the p30-2 polynucleotide.

[0034]FIG. 23B shows one embodiment of the P30-3 protein, FIG. 23A shows one embodiment of the p30-3 polynucleotide.

[0035]FIG. 24B shows one embodiment of the P30-4 protein, FIG. 22A shows one embodiment of the p30-4 polynucleotide.

[0036]FIG. 25B shows one embodiment of the P30-5 protein, FIG. 22A shows one embodiment of the p30-5 polynucleotide.

[0037]FIG. 26B shows one embodiment of the P30-6 protein, FIG. 26A shows one embodiment of the p30-6 polynucleotide.

[0038]FIG. 27B shows one embodiment of the P30-7 protein, FIG. 27A shows one embodiment of the p30-7 polynucleotide.

[0039]FIG. 28B shows one embodiment of the P30-8 protein, FIG. 28A shows one embodiment of the p30-8 polynucleotide.

[0040]FIG. 29B shows one embodiment of a portion of the P30-9 protein, FIG. 29A shows one embodiment of the p30-9 polynucleotide.

[0041]FIG. 30B shows one embodiment of a portion of the P30-10 protein, FIG. 30A shows one embodiment of the p30-10 polynucleotide encoding such protein.

[0042]FIG. 31B shows one embodiment of a portion of the P30-11 protein, FIG. 31A shows one embodiment of the p30-11 polynucleotide.

[0043]FIG. 32B shows one embodiment of a portion of the P30-12 protein, FIG. 32A shows one embodiment of the p30-12 polynucleotide.

[0044]FIG. 33B shows one embodiment of a portion of the OMP-1H protein, FIG. 33A shows one embodiment of the OMP-1H polynucleotide.

[0045]FIG. 34 depicts the amino acid sequences alignment of six E. chaffeensis OMP-1s and Cowdria ruminantium MAP-1. Aligned positions of identical amino acids with OMP-1F are shown with dots. The sequence of C. ruminantium MAP-1 is from the report of Van Vliet et al (1994) Molecular cloning, sequence analysis, and expression of the gene encoding the immunodominant 32-kilodalton protein of Cowdria ruminantium. Infect. Immun. 62:1451-1456. Gaps indicated by dashes were introduced for optimal alignment of all proteins. Bars indicate semivariable region (SV) and three hypervariable regions (HV1, HV2, and HV3).

DETAILED DESCRIPTION OF THE INVENTION

[0046] The present invention provides a group of outer membrane proteins of E. chaffeensis, OMP proteins, and a group of outer membrane proteins of E. canis, the P30F proteins. The mature OMP-1 protein of E. chaffeensis has a molecular weight of about 27.7 kDa and comprises amino acid 26 through amino acid 281 of the sequence shown in FIG. 3B, SEQ ID NO: 2. The mature OMP-1B protein of E. chaffeensis has a molecular weight of about 28.2 kDa and comprises amino acid 26 through amino acid 283 of the sequence shown in FIG. 4B, SEQ ID NO: 4. The mature OMP-1C protein of E. chaffeensis has a molecular weight of about 27.6 kDa and comprises amino acid 26 through amino acid 280 of the sequence shown in FIG. 5B, SEQ ID NO: 6. The mature OMP-1D protein of E. chaffeensis has a molecular weight of about 28.7 and comprises amino acid 26 through amino acid 286 of the sequence shown in FIG. 6B, SEQ ID NO: 8. The mature OMP-1E protein of E. chaffeensis has a molecular weight of about 27.8 kDa and comprises amino acid 26 through amino acid 278 of the sequence shown in FIG. 7B, SEQ ID NO: 10. The mature OMP-1F protein of E. chaffeensis has a molecular weight of about 27.9 kDa and comprises amino acid 26 through amino acid 280 of the sequence shown in FIG. 8B, SEQ ID NO: 12. The mature OMP-1A protein of E. chaffeensis has a molecular weight of about 29.6 kDa and comprises amino acid 31 through amino acid 279 of the sequence shown in FIG. 9B, SEQ ID NO: 14. The mature OMP-1R protein of E. chaffeensis has a molecular weight of about 19.7 kDa and comprises the amino acid 29 through amino acid 196 of the sequence shown in FIG. 10B, SEQ ID NO: 16. The mature OMP-1S protein of E. chaffeensis has a molecular weight of about 29.2 kDa and comprises amino acid 26 through amino acid 291 of the sequence shown in FIG. 11B, SEQ ID NO: 18. The OMP-1T protein of E. chaffeensis comprises the amino acid sequence shown in FIG. 12B, SEQ ID NO: 20. The mature OMP-1U protein of E. chaffeensis has a molecular weight of about 30.6 kDa and comprises amino acid 26 through amino acid 295 of the sequence shown in FIG. 13B, SEQ ID NO: 22. The mature OMP-1V protein of E. chaffeensis has a molecular weight of about 28.0 kD and comprises amino acid 27 through amino acid 279 shown in FIG. 14B, SEQ ID NO: 24. The mature OMP-1W protein of E. chaffeensis has a molecular weight of about 28.8 kDa and comprises amino acid 30 through amino acid 283 of the sequence shown in FIG. 15B, SEQ ID NO: 26. The mature OMP-1X protein of E. chaffeensis has a molecular weight of about 27.8 kDa and comprises amino acid 25 through amino acid 275 of the sequence shown in FIG. 16B, SEQ ID NO: 28. The mature OMP-1Y protein of E. chaffeensis has a molecular weight about 28.8 kDa and comprises amino acid 28 through amino acid 285 of the sequence shown in FIG. 17B, SEQ ID NO: 30. The mature OMP-1Z protein of E. chaffeensis has a molecular weight of about 30.2 kDa and comprises amino acid 27 through amino acid 300 of the sequence shown in FIG. 18B, SEQ ID NO: 50. The mature OMP-1H protein has a molecular weight of about 30.2 kDa and comprises the amino acid 27 through amino acid 298 of sequence shown in FIG. 33B, SEQ ID NO: 52.

[0047] The mature P30 protein of E. canis has a molecular weight of about 28.8 kDa and comprises amino acid 26 through amino acid 288 of the sequence shown in FIG. 19B, SEQ ID NO: 32. The mature P30a protein of E. canis has a molecular weight of about 29.0 kDa and comprises amino acid 26 through amino acid 287 of the sequence shown in FIG. 20B, SEQ ID NO: 34. The mature P30-1 protein of E. canis has a molecular weight of about 27.7 kDa and comprises amino acid 55 through amino acid 307 of the sequence shown in FIG. 21B, SEQ ID NO: 36. The mature P30-2 protein of E. canis has a molecular weight of about 28.0 kDa and comprises amino acid 26 through amino acid 280 of the sequence shown in FIG. 22B, SEQ ID NO: 38. The mature P30-3 protein of E. canis has a molecular weight of about 28.7 kDa and comprises amino acid 26 through amino acid 283 of the sequence shown in FIG. 23B, SEQ ID NO: 40. The mature P30-4 protein of E. canis has a molecular weight of about 28.0 kDa and comprises amino acid 26 through amino acid 276 of the sequence shown in FIG. 24B, SEQ ID NO: 42. The mature P30-5 protein of E. canis has a molecular weight of about 29.4 kDa and comprises amino acid 27 through amino acid 293 of the sequence shown in FIG. 25B, SEQ ID NO: 44. The mature P30-6 protein of E. canis has a molecular weight of about 29.4 kDa and comprises amino acid 31 through amino acid 293 of the sequence shown in FIG. 26B, SEQ ID NO: 54. The mature P30-7 protein of E. canis has a molecular weight of about 29.9 kDa and comprises amino acid 31 through amino acid 296 of the sequence shown in FIG. 27B, SEQ ID NO: 56. The mature P30-8 protein of E. canis has a molecular weight of about 30.3 kDa and comprises amino acid 27 through amino acid 299 of the sequence shown in FIG. 28B, SEQ ID NO: 46. The mature P30-9 protein of E. canis has a molecular weight of about 28.6 kDa and comprises amino acid 27 through amino acid 281 of the sequence shown in FIG. 29B, SEQ ID NO: 58. The mature P30-10 protein of E. canis has a molecular weight of about 28.1 kDa and comprises amino acid 26 through amino acid 280 of the sequence shown in FIG. 30B, SEQ ID NO: 48. The mature P30-11 protein of E. canis has a molecular weight of about 28.6 kDa and comprises the amino acid 26 through amino acid 279 of sequence shown in FIG. 31B, SEQ ID NO: 60. The P30-12 protein of E. canis has a molecular weight of at least 27.3 kDa and comprises the amino acid sequence shown in FIG. 32B, SEQ ID NO: 62.

[0048] The present invention also encompasses variants of the OMP proteins shown in FIGS. 3-18 and 33 and variants of the P30F proteins shown in FIGS. 19-32. A “variant” as used herein, refers to a protein whose amino acid sequence is similar to one the amino acid sequences shown in FIGS. 3-33, hereinafter referred to as the reference amino acid sequence, but does not have 100% identity with the respective reference sequence. The variant protein has an altered sequence in which one or more of the amino acids in the reference sequence is deleted or substituted, or one or more amino acids are inserted into the sequence of the reference amino acid sequence. As a result of the alterations, the variant protein has an amino acid sequence which is at least 95% identical to the reference sequence, preferably, at least 97% identical, more preferably at least 98% identical, most preferably at least 99% identical to the reference sequence. Variant sequences which are at least 95% identical have no more than 5 alterations, i.e. any combination of deletions, insertions or substitutions, per 100 amino acids of the reference sequence. Percent identity is determined by comparing the amino acid sequence of the variant with the reference sequence using MEGALIGN project in the DNA STAR program. Sequences are aligned for identity calculations using the method of the software basic local alignment search tool in the BLAST network service (the National Center for Biotechnology Information, Bethesda, Md.) which employs the method of Altschul, S. F., Gish, W., Miller, W., Myers, E. W. & Lipman, D. J. (1990) J. Mol. Biol. 215, 403-410. Identities are calculated by the Align program (DNAstar, Inc.) In all cases, internal gaps and amino acid insertions in the candidate sequence as aligned are not ignored when making the identity calculation.

[0049] While it is possible to have nonconservative amino acid substitutions, it is preferred that the substitutions be conservative amino acid substitutions, in which the substituted amino acid has similar structural or chemical properties with the corresponding amino acid in the reference sequence. By way of example, conservative amino acid substitutions involve substitution of one aliphatic or hydrophobic amino acids, e.g. alanine, valine, leucine and isoleucine, with another; substitution of one hydroxyl-containing amino acid, e.g. serine and threonine, with another; substitution of one acidic residue, e.g. glutamic acid or aspartic acid, with another; replacement of one amide-containing residue, e.g. asparagine and glutamine, with another; replacement of one aromatic residue, e.g. phenylalanine and tyrosine, with another; replacement of one basic residue, e.g. lysine, arginine and histidine, with another; and replacement of one small amino acid, e.g., alanine, serine, threonine, methionine, and glycine, with another.

[0050] The alterations are designed not to abolish the immunoreactivity of the variant protein with antibodies that bind to the reference protein. Guidance in determining which amino acid residues may be substituted, inserted or deleted without abolishing such immunoreactivity of the variant protein are found using computer programs well known in the art, for example, DNASTAR software. A variant of the OMP-1 protein is set forth in SEQ ID NO: 67 where the alanine at position 280 is replaced with a valine.

[0051] The present invention also encompasses fusion proteins in which a tag or one or more amino acids, preferably from about 2 to 65 amino acids, more preferably from about 34 to about 62 amino acids are added to the amino or carboxy terminus of the amino acid sequence of an OMP protein, a P30F protein, or a variant of such protein. Typically, such additions are made to stabilize the resulting fusion protein or to simplify purification of an expressed recombinant form of the corresponding OMP protein, P30F protein or variant of such protein. Such tags are known in the art. Representative examples of such tags include sequences which encode a series of histidine residues, the Herpes simplex glycoprotein D, or glutathione S-transferase.

[0052] The present invention also encompasses OMP proteins and P30F proteins in which one or more amino acids, preferably no more than 10 amino acids, in the respective OMP protein or P30F are altered by posttranslation processes or synthetic methods. Examples of such modifications include, but are not limited to, acetylation, amidation, ADP-ribosylation, covalent attachment of flavin, covalent attachment of a heme moiety, covalent attachment of a nucleotide or a lipid, cross-linking gamma-carboxylation, glycosylation, hydroxylation, iodination, methylation, myristoylation, oxidation, pegylation, proteolytic processing, phosphorylation, prenylation, racemization, sulfation, and transfer-RNA mediated additions of amino acids to proteins such as arginylation and ubiquitination.

[0053] The OMP proteins, particularly a recombinant form of OMP-1, are immunogenic and, thus are useful for preparing antibodies. Such antibodies are useful for immunolabeling isolates of E. chaffeensis and for detecting the presence of E. chaffeensis in body fluids, tissues, and particularly in monocytes and macrophages. The OMP proteins, particularly OMP-1, are also useful for detecting antibodies to E. chaffeensis in the blood of patients with clinical signs of ehrlichiosis. The OMP proteins , particularly OMP-1, are also useful immunogens for raising antibodies that are capable of reducing the level of infection in an immunized mammal that has been infected with E. chaffeensis. The OMP proteins are also useful in a vaccine for protecting against infection with E. chaffeensis.

[0054] The P30F proteins, particularly recombinant forms of P30, are immunogenic and are, thus, useful for preparing antibodies that are useful for immunolabeling isolates of E. canis. The P30 protein is also useful for diagnosing canine ehrlichiosis in mammals, particularly in members of the family Canidae, most particularly in dogs and for diagnosing infections with E. chaffeensis in humans. The P30F proteins are also useful immunogens for raising antibodies that reduce the level of infection in an immunized mammal that has been infected with E. canis. The P30F proteins are also useful in a vaccine for protecting animals against infection with E. canis.

[0055] In another aspect, the present invention provides a polypeptide which comprises a fragment of the OMP1 protein, hereinafter referred to as “rOMP-1”. The rOMP-1 polypeptide weighs approximately 31 kDa and comprises all but of the first 5 amino acids of mature OMP-1 protein. The rOMP-1 polypeptide comprises the amino acid sequence extending from amino acid 6 through amino acid 251 of the amino acid sequence shown in FIG. 1, SEQ ID NO. 2. The present invention also embraces polypeptides where one or more of the amino acids in the sequence extending from amino acid 1 or 6 through amino acid 251 FIG. 1 are replaced by conservative amino acid residues. The present invention also relates to variant of rOMP-1 that have an amino acid sequence identity of at least 95%, more preferably at least 97%, and most preferably of at least 99% with the amino acid sequence extending from amino acid 6 through amino acid 251 of the OMP-1 protein and which derivative binds to antibodies in sera from humans infected with E. chaffeensis.

[0056] Polynucleotides

[0057] The present invention also provides isolated polynucleotides which encode the OMP proteins and the P30F proteins. The OMP-1 polynucleotide encodes the OMP-1 protein of E. chaffeensis, FIG. 3A shows one embodiment of the OMP-1 polynucleotide, SEQ ID NO: 1. The OMP-1B polynucleotide encodes the OMP-1B protein of E. chaffeensis ; FIG. 4A shows one embodiment of the OMP-1B polynucleotide, SEQ ID NO: 3. The OMP-1C polynucleotide encodes the OMP-1C protein of E. chaffeensis , FIG. 5A shows one embodiment of the OMP-1C polynucleotide; SEQ ID NO: 5. The OMP-1D polynucleotide encodes the OMP-1D protein of E. chaffeensis ; FIG. 6A shows one embodiment of the OMP-1D polynucleotide, SEQ ID NO: 7. The OMP-1E polynucleotide encodes the OMP-1E protein of E. chaffeensis ; FIG. 7A shows one embodiment of the OMP-1E polynucleotide, SEQ ID NO: 9. The OMP-1F polynucleotide encodes the OMP-1F protein of E. chaffeensis ; FIG. 8A shows one embodiment of the OMP-1F polynucleotide, SEQ ID NO: 11. The OMP-1A polynucleotide encodes the OMP-1A protein of E. chaffeensis ; FIG. 9A shows one embodiment of the OMP-1A polynucleotide, SEQ ID NO: 13. The OMP-1R polynucleotide encodes the OMP-1R protein, FIG. 10A shows one embodiment of a portion of the OMP-1R polynucleotide, SEQ ID NO: 15. The OMP-1S polynucleotide encodes the OMP-1S protein of E. chaffeensis ; FIG. 11A shows one embodiment of a portion of the OMP-1S polynucleotide, SEQ ID NO: 17. The OMP-1T polynucleotide encodes the OMP-1T protein of E. chaffeensis ; FIG. 12A shows one embodiment of a portion of the OMP-1T polynucleotide, SEQ ID NO: 19. The OMP-1U polynucleotide encodes the OMP-1U protein of E. chaffeensis ; FIG. 13A shows one embodiment of the OMP-1U polynucleotide, SEQ ID NO: 21. The OMP-1V polynucleotide encodes the OMP-1V protein of E. chaffeensis ; FIG. 14A shows one embodiment of the OMP-1V polynucleotide, SEQ ID NO: 23. The OMP-1W polynucleotide encodes the OMP-1W protein of E. chaffeensis ; FIG. 15A shows one embodiment of the OMP-1W polynucleotide, SEQ ID NO: 25. The OMP-1X polynucleotide encodes an OMP-1X protein of E. chaffeensis ; FIG. 16A shows one embodiment of the OMP-1X polynucleotide, SEQ ID NO 27. The OMP-1Y polynucleotide encodes the OMP-1Y protein of E. chaffeensis ; FIG. 17A shows one embodiment of the OMP-1Y polynucleotide, SEQ ID NO 29. The OMP-1Z polynucleotide encodes the OMP-1Z protein of E. chaffeensis ; FIG. 18A shows one embodiment of an OMP-1Z polynucleotide encoding such polypeptide, SEQ ID NO: 49. The OMP-1H polynucleotide encodes the OMP-1H protein of E. chaffeensis ; FIG. 33A shows one embodiment of a portion of the OMP-1H polynucleotide, SEQ ID NO: 51.

[0058] The p30 polynucleotide encodes the P30 protein of E. canis, FIG. 19A shows one embodiment of the p30 polynucleotide, SEQ ID NO: 31. The p30a polynucleotide encodes the P30a protein of E. canis, FIG. 20A shows one embodiment of the p30a polynucleotide, SEQ ID NO: 33. The p30-1 polynucleotide encodes the P30-1 protein of E. canis; FIG. 21A shows one embodiment of the p30-1 polynucleotide, SEQ ID NO: 35. The p30-2 polynucleotide encodes the P30-2 protein of E. canis; FIG. 22A shows one embodiment of the p30-2 polynucleotide, SEQ ID NO: 37. The p30-3 polynucleotide encodes the P30-3 protein of E.canis; FIG. 23A shows one embodiment of the p30-3 polynucleotide, SEQ ID NO: 39. The p30-4 polynucleotide encodes the P30-4 protein of E. canis, FIG. 24A shows one embodiment of the p30-4 polynucleotide, SEQ ID NO: 41. The p30-5 polynucleotide encodes the P30-5 protein of E. canis, FIG. 25A shows one embodiment of the p30-5 polynucleotide, SEQ ID NO: 43. The p30-6 polynucleotide encodes the P30-6 protein, FIG. 26A shows one embodiment of the p30-6 polynucleotide, SEQ ID NO: 53. The p30-7 polynucleotide encodes the P30-7 protein of E. canis; FIG. 27A shows one embodiment of the p30-7 polynucleotide, SEQ ID NO: 55. The p30-8 polynucleotide encodes the P30-8 protein of E. canis; FIG. 28A shows one embodiment of the p30-8 polynucleotide, SEQ ID NO: 45. The p30-9 polynucleotide encodes the P30-9 protein of E. canis; FIG. 29A shows one embodiment of a portion of the p30-9 polynucleotide, SEQ ID NO: 57. The p30-10 polynucleotide encodes the P30-10 protein of E. canis, FIG. 30A shows one embodiment of a portion of the p30-10 polynucleotide, SEQ ID NO: 47. The p30-11 polynucleotide encodes the P30-11 protein of E. canis; FIG. 31A shows one embodiment of a portion of the p30-11 polynucleotide, SEQ ID NO: 59. The p30-12 polynucleotide encodes the P30-12 protein of E. canis; FIG. 32A shows one embodiment of a portion of the p30-12 polynucleotide, SEQ ID NO: 61.

[0059] The polynucleotides are useful for producing the outer membrane proteins of E. chaffeensis and E. canis. For example, an RNA molecule encoding the outer membrane protein OMP-1 is used in a cell-free translation systems to prepare OMP-1. Alternatively, a DNA molecule encoding the outer membrane protein is introduced into an expression vector and used to transform cells. Suitable expression vectors include for example chromosomal, nonchromosomal and synthetic DNA sequences, e.g., derivatives of SV40, bacterial plasmids, phage DNAs; yeast plasmids, vectors derived from combinations of plasmids and phage DNAs, viral DNA such as vaccinia, adenovirus, fowl pox virus, and pseudorabies. The DNA sequence is introduced into the expression vector by conventional procedures.

[0060] Accordingly, the present invention also relates to recombinant constructs comprising one or more of the polynucleotide sequences. Suitable constructs include, for example, vectors, such as a plasmid, phagemid, or viral vector, into which a sequence that encodes the outer membrane protein has been inserted. In the expression vector, the DNA sequence which encodes the outer membrane protein is operatively linked to an expression control sequence, i.e., a promoter, which directs mRNA synthesis. Representative examples of such promoters, include the LTR or SV40 promoter, the E. coli lac or trp, the phage lambda PL promoter and other promoters known to control expression of genes in prokaryotic or eukaryotic cells or in viruses. The promoter may also be the natural promoter of the outer membrane protein coding sequence. The expression vector also contains a ribosome binding site for translation initiation and a transcription terminator. Preferably, the recombinant expression vectors also include an origin of replication and a selectable marker, such as for example, the ampicillin resistance gene of E. coli to permit selection of transformed cells, i.e. cells that are expressing the heterologous DNA sequences. The polynucleotide sequence encoding the outer membrane protein is incorporated into the vector in frame with translation initiation and termination sequences. Optionally, the sequence encodes a fusion outer membrane protein which includes an N-terminal or C-terminal peptide or tag that stabilizes or simplifies purification of the expressed recombinant product. Representative examples of such tags include sequences which encode a series of histidine residues, the Herpes simplex glycoprotein D, or glutathione S-transferase.

[0061] Polynucleotides encoding the OMP proteins and the P30F proteins are also useful for designing hybridization probes for isolating and identifying cDNA clones and genomic clones encoding the OMP proteins, the P30F proteins or allelic forms thereof. Such hybridization techniques are known to those of skill in the art. The sequences that encode the OMP proteins and the P30F proteins are also useful for designing primers for polymerase chain reaction (PCR), a technique useful for obtaining large quantities of cDNA molecules that encode the OMP proteins and the P30F proteins.

[0062] Also encompassed by the present invention, are single stranded polynucleotides, hereinafter referred to as antisense polynucleotides, having sequences which are complementary to the DNA and RNA sequences which encode the OMP proteins and the P30F proteins. The term complementary as used herein refers to the natural binding of the polynucleotides under permissive salt and temperature conditions by base pairing,

[0063] The present invention also encompasses oligonucleotides that are used as primers in polymerase chain reaction (PCR) technologies to amplify transcripts of the genes which encode the OMP proteins, the P30F proteins or portions of such transcripts. Preferably, the primers comprise 18-30 nucleotides, more preferably 19-25 nucleotides. Preferably, the primers have a G+C content of 40% or greater. Such oligonucleotides are at least 98% complementary with a portion of the DNA strand, i.e., the sense strand, which encodes the OMP protein or the P30F protein, or a portion of its corresponding antisense strand. Preferably, the primer has at least 99% complementarity, more preferably 100% complementarity, with such sense strand or its corresponding antisense strand. Primers which are which have 100% complementarity with the antisense strand of a double-stranded DNA molecule which encodes an OMP protein or a P30F protein have a sequence which is identical to a sequence contained within the sense strand. The identity of primers which are 15 nucleotides in length and have full complementarity with a portion of the antisense strand of a double-stranded DNA molecule which encodes the OMP-1 protein is determined using the nucleotide sequence, SEQ ID NO: 1, shown in FIG. 3A and described by the general formula a-b, where a is any integer between 1 to 843, where b is equal to a+14, and where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO: 1.

[0064] The present invention also encompasses oligonucleotides that are useful as hybridization probes for detecting transcripts of the genes which encode the OMP proteins and P30F proteins or for mapping of the genes which encode the OMP proteins and P30F proteins. Preferably, such oligonucleotides comprise at least 210 nucleotides, more preferably at least 230, most preferably from about 210 to 280 nucleotides. Such hybridization probes have a sequence which is at least 90% complementary with a sequence contained within the sense strand of a DNA molecule which encodes each of OMP proteins and P30F proteins or with a sequence contained within its corresponding antisense strand. Such hybridization probes bind to the sense strand under stringent conditions. The term “stringent conditions” as used herein is the binding which occurs within a range from about Tm 5° C. (5° C. below the melting temperature Tm of the probe) to about 20° C. to 25° C. below Tm. The probes are used in Northern assays to detect transcripts of OMP and P30F homologous genes and in Southern assays to detect OMP and P30F homologous genes. The identity of probes which are 200 nucleotides in length and have full complementarity with a portion of the antisense strand of a double-stranded DNA molecule which encodes the OMP-1 protein is determined using the nucleotide sequence, SEQ ID NO: 1, shown in FIG. 3A and described by the general formula a-b, where a is any integer between 1 to 843, b is equal to a+200, and where both a and b correspond to the positions of nucleotide residues shown in SEQ ID NO: 1.

[0065] The present invention also encompasses isolated polynucleotides which are alleles of the genes which encode the OMP proteins and the P30F proteins. As used herein, an allele or allelic sequence is an alternative form of the gene which may result from one or more mutations in the sequences which encode the OMP proteins and P30F proteins. Such mutations typically arise from natural addition, deletion of substitution of nucleotides in the open reading frame sequences. Any gene may have none, one, or several allelic forms. Such alleles are identified using conventional techniques, such as for example screening libraries with probes having sequences identical to or complementary with one or more OMP or P30F polynucleotides.

[0066] The present invention also encompasses altered polynucleotides which encode OMP proteins and P30F proteins. Such alterations include deletions, additions, or substitutions. Such alterations may produce a silent change and result in an OMP protein or P30F protein having the same amino acid sequence as the OMP protein or P30F protein encoded by the unaltered polynucleotide. Such alterations may produce a nucleotide sequence possessing non-naturally occurring codons. For example, codons preferred by a particular prokaryotic or eucaryotic host may be incorporated into the nucleotide sequences shown in FIGS. 3-33 to increase the rate of expression of the proteins encoded by such sequences. Such alterations may also introduce new restriction sites into the sequence or result in the production of an OMP protein variant or P30F protein variant. Typically, such alterations are accomplished using site-directed mutagenesis.

[0067] Antibodies

[0068] In another aspect, the present invention relates to antibodies which are specific for and bind to at least one OMP protein or P30F protein. Such antibodies are useful research tools for identifying cells, particularly monocytes or macrophages, infected with E. chaffeensis or E. canis and for purifying the major outer membrane protein of E. chaffeensis or E. canis from partially purified preparations by affinity chromatography. Such antibodies are also useful for identifying bacterial colonies, particularly colonies of genetically-engineered bacteria, that are expressing the major outer membrane protein of E. chaffeensis or E. canis.

[0069] Kits

[0070] The present invention also relates to kits containing reagents for diagnosing E. chaffeensis and E. canis. The kit comprises one or more OMP proteins, or one or more E. canis proteins, or antigenic fragments thereof. For ease of detection, it is preferred that the OMP protein or P30F proteins be attached to a substrate such as a column, plastic dish, matrix, or membrane, preferably nitrocellulose. The kit may further comprise a biomolecule, preferably a secondary antibody, for detecting interactions between the isolated OMP protein or P30F protein and antibodies in a patient sample. Preferably, the biomolecule is coupled to a detectable tag such as an enzyme, chromophore, fluorophore, or radio-isotope. The kit is used by contacting a patient sample with the OMP protein or P30F protein under conditions that permit formation of antigen-antibody complexes. Then the biomolecule is added and the presence or absence of any resulting antigen-antibody complexes is detected by assaying for a change in the sample, for example, by observing the formation of a precipitate in the sample, the presence of radioactivity on the substrate, or a color change in the sample or on the substrate.

[0071] Diagnostic Method

[0072] The present invention also provides a method for detecting antibodies to the E. chaffeensis or E. canis in a sample of a bodily fluid from a patient. The method comprises providing an isolated outer membrane protein of E. chaffeensis or E. canis, particularly a recombinant form of the isolated protein, contacting the outer membrane protein or polypeptide with a sample taken from the patient; and assaying for the formation of a complex between the outer membrane protein or polypeptide and antibodies in the sample. For ease of detection, it is preferred that the isolated protein or polypeptide be attached to a substrate such as a column, plastic dish, matrix, or membrane, preferably nitrocellulose. The sample may be a tissue or a biological fluid, including urine, whole blood, or exudate, preferably serum. The sample may be untreated, subjected to precipitation, fractionation, separation, or purification before combining with the isolated protein or peptide. Interactions between antibodies in the sample and the isolated protein or peptide are detected by radiometric, colorimetric, or fluorometric means, size-separation, or precipitation. Preferably, detection of the antibody-outer membrane protein complex is by addition of a secondary antibody that is coupled to a detectable tag, such as for example, an enzyme, fluorophore, or chromophore. Formation of the complex is indicative of the presence of anti-E chaffeensis or anti-E canis antibodies, either IgM or IgG, in the patient. Thus, the method is used to determine whether a patient is infected with E. chaffeensis or E. canis.

[0073] Preferably, the method employs an enzyme-linked immunosorbent assay (ELISA) or a Western immunoblot procedure. Such methods are relatively simple to perform and do not require special equipment as long as membrane strips are coated with a high quality antigen. Accordingly, it is more advantageous to use a recombinant form of the outer membrane protein of E. chaffeensis or E. canis since such proteins, typically, are more pure and consistent in quality than a purified form of such protein.

[0074] Immunogenic Composition

[0075] The present invention also relates to immunogenic compositions comprising one or more OMP protein of E. chaffeensis and a pharmaceutically acceptable adjuvant and to immunogenic compositions comprising one or more P30F proteins of E. canis and a pharmaceutically acceptable adjuvant, which, preferably, enhances the immunogenic activity of the outer membrane protein in the host animal.

[0076] Preparing the OMP Proteins and the P30F Proteins

[0077] The OMP proteins and P30F proteins may be produced by conventional peptide synthesizers. The OMP proteins and P30F proteins may also be produced using cell-free translation systems and RNA molecules derived from DNA constructs that encode the OMP proteins and P30F proteins. Alternatively, OMP proteins and P30F proteins are made by transfecting host cells with expression vectors that comprise a DNA sequence that encodes the respective OMP protein or P30F protein and then inducing expression of the protein in the host cells. For recombinant production, recombinant constructs comprising one or more of the sequences which encode the OMP protein or P30F protein are introduced into host cells by conventional methods such as calcium phosphate transfection, DEAE-dextran mediated transfection, transvection, microinjection, cationic lipid-mediated transfection, electroporation, transduction, scrape lading, ballistic introduction or infection.

[0078] The OMP proteins or P30F proteins may be expressed in suitable host cells, such as for example, mammalian cells, yeast, bacteria, or other cells under the control of appropriate promoters using conventional techniques. Following transformation of the suitable host strain and growth of the host strain to an appropriate cell density, the cells are harvested by centrifugation, disrupted by physical or chemical means, and the resulting crude extract retained for further purification of the OMP protein or P30F protein.

[0079] Conventional procedures for isolating recombinant proteins from transformed host cells, such as isolation by initial extraction from cell pellets or from cell culture medium, followed by salting-out, and one or more chromatography steps, including aqueous ion exchange chromatography, size exclusion chromatography steps, and high performance liquid chromatography (HPLC), and affinity chromatography may be used to isolate recombinant OMP protein or P30F protein

[0080] Preparation of Antibodies

[0081] The OMP proteins, P30F proteins, and variants thereof are used as immunogens to produce antibodies immunospecific for one or more OMP protein or one or more P30F protein. The term “immunospecific” means the antibodies have substantially greater affinity for one or more OMP protein or P30F protein than for other proteins. Such antibodies may include, but are not limited to, polyclonal, monoclonal, chimeric, single chain, and Fab fragments.

[0082] Polyclonal antibodies are generated using conventional techniques by administering the OMP protein or P30F protein, or a chimeric molecule to a host animal. Depending on the host species, various adjuvants may be used to increase immunological response. Among adjuvants used in humans, BCG (bacilli Calmette-Guerin, and Corynebacterium parvum are especially preferable. Conventional protocols are also used to collect blood from the immunized animals and to isolate the serum and or the IgG fraction from the blood.

[0083] For preparation of monoclonal antibodies, conventional hybridoma techniques are used. Such antibodies are produced by continuous cell lines in culture. Suitable techniques for preparing monoclonal antibodies include, but are not limited to, the hybridoma technique, the human B-cell hybridoma technique, and the EBV hybridoma technique.

[0084] Various immunoassays may be used for screening to identify antibodies having the desired specificity. These include protocols which involve competitive binding or immunoradiometric assays and typically involve the measurement of complex formation between the respective OMP protein or P30F protein and the antibody.

[0085] Polynucleotides that Encode OMP Proteins and P30F Proteins

[0086] Polynucleotides comprising sequences encoding an OMP protein or P30F protein may be synthesized in whole or in part using chemical methods. Polynucleotides which encode an OMP protein or P30F protein, particularly alleles of the genes which encode an OMP protein or P30F protein, may be obtained by screening a genomic library of an E. chaffeensis or E. canis isolate with a probe comprising sequences identical or complementary to the sequences shown in FIGS. 3-33 or with antibodies immunospecific for a OMP protein or P30F protein to identify clones containing such polynucleotide.

[0087] Polynucleotides which Encode OMP-1 Protein and P30 Protein

[0088] A. Isolation of the Outer Membrane Proteins

[0089]E. chaffeensis Arkansas strain and E. canis Oklahoma strain were cultivated in the DH82 dog macrophage cell line and purified by Percoll density gradient centrifugation. Purified ehrlichiae (100 μg) were suspended with 10 mM sodium phosphate buffer, pH 7.4, containing 0.1% Sodium N-lauroyl sarcosine (Sarkosyl) [Sigma, St. Louis, Mo.], 50 μg/ml each DNase I (Sigma) and RNase A (Sigma), and 2.5 mM MgCl₂. After incubation at 37° for 30 min, the sample was separated by centrifugation at 10,000×g for 1 h into the soluble supernatant and the insoluble precipitate. The insoluble pellet was resuspended 2 to 3 times with 0.1% Sarkosyl and centrifuged. The final pellet was analyzed by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) and by electron microscopy.

[0090] Transmission electron microscopy revealed that the purified ehrlichial fraction consists of a mixture of electron dense and light forms of E. chaffeensis with slight disintegration of inner membrane. Ehrlichiae were not surrounded with the host inclusion membrane. Various sizes of membrane vesicles (<1 μm) without significant ribosomes or nuclear materials were observed in the Sarkosyl-insoluble fraction from the organism. Succinic debydrogenase (inner membrane marker enzyme of gram negative bacteria) activities were at less than the detection limit (1 n moles/min/mg of protein) in the Sarkosyl-insoluble fraction compared to approximately 10 n moles/min/mg of protein in the Percoll-purified organisms, suggesting that the insoluble fraction primarily consisted of the outer membrane of E. chaffeensis.

[0091] Analysis of the Sarkosyl-soluble, and insoluble fraction of E. chaffeensis by SDS-PAGE suggested that proteins of 30-kDa range in the insoluble fraction represent the major outer membrane proteins of this organism. Analysis of the Sarkosyl-soluble, and insoluble fraction of E. canis by SDS-PAGE suggested that proteins of 30-kDa range in the insoluble fraction represent the major outer membrane proteins of this organism also. E. canis was antigenically cross reactive with E. chaffeensis. These findings indicate that the 30-kDa range proteins represent the major outer membrane proteins of these two Ehrlichia spp.

[0092] To improve resolution of the outer membrane proteins, proteins in the Sarkosyl-insoluble pellet prepared from 400 μg of purified E. chaffeensis were separated by a reversed-discontinuous (Rd) SDS-PAGE (2.5-cm-long 17% gel on top of 11-cm-long 12% gel). At least five proteins of 30-kDa range in E. chaffeensis (P23, P25, P27, P28, and P29) were resolved from the Sarkosyl-insoluble proteins.

[0093] B. Cloning and Sequencing of the omp-1 Gene

[0094] The portion of the membrane containing bound proteins was excised and analyzed with an Applied Biosystems protein sequencer (Model 470). The N-terminal amino acid sequence of OMP-1 protein was determined as D P A G S G I N G N F Y I S G K Y M P, SEQ ID NO: 63. Based on 6th to 12th amino acids of this sequence, a forward primer, FECH1, having the sequence: 5′-CGGGATCCGAATTCGG(A/T/G/C)AT(A/T/C)AA(T/C)GG(A/T/G/C)AA(T/C)TT(T/C)TA-3′. SEQ ID NO: 64 was designed. Amino acids at the 1 to 5 positions of the N terminus of OMP-1 were not included in this primer design. For insertion into an expression vector, a 14-bp sequence (underlined) was added at the 5′ end of primer to create an EcoRI and a BamHI site. The reverse primer, RECH2, which includes a NotI site at the 5′ end for ligation into an expression vector had the sequence: 5′-AGCGGCCGCTTA(A/G)AA(T/C)A(C/G) (A/G)AA (C/T)CT T(C/G)C TCC-3′. SEQ ID NO: 65.

[0095] Genomic DNA of E. chaffeensis was isolated from purified organisms. PCR amplification with FECH1 and RECH2 primers was performed using a Perkin-Elmer Cetus DNA Thermal Cycler (model 480). A 0.8-kb amplified product was cloned in the pCRII vector of a TA closing kit, as described by the manufacturer (Invitrogen Co., San Diego, Calif.). The clone obtained was designated pCRIIp28. Both strands of the inserted DNA were sequenced by a dideoxy-termination method with an Applied Biosystems 373A DNA sequencer.

[0096] The 0.8-kb DNA fragment containing a partial OMP-1 gene, cloned in pCRIIp28, had an open reading frame (ORF) of 756 bp encoding a 251-amino acid recombinant protein (including both PCR primer regions) with a molecular mass of 27.2 kDa. The nucleotide sequence of the open reading frame, and the amino acid sequence of the polypeptide of the partial OMP-1 protein, are shown in FIG. 1.

[0097] A DNA fragment comprising the partial p30 gene was prepared in a similar manner, i.e., by PCR amplification of genomic DNA of E. canis using the forward primer, FECH1, which is described above, and a reverse primer, REC1, which is complimentary to the DNA sequence corresponding to amino acid positions 185 to 191 of the mature OMP-1 of E. chaffeensis. The sequence of REC1 is 5′-ACCTAACTTTCCTTGGTAAG-3′, SEQ ID NO: 66.

[0098] Genomic DNA of E. canis was isolated from the purified organism. PCR amplification was performed by using a Perkin-Elmer Cetus DNA Thermal Cycler (model 480). The 0.6-kb products were amplified with the FECH1-REC1 primer pair and were cloned into the pCRII vector of a TA cloning kit (Invitrogen Co., San Diego, Calif.). The clone obtained by the primer pair was designated pCRIIp30. Both strands of the insert DNA were sequenced by a dideoxy termination method with an Applied Biosystems 373 DNA sequencer.

[0099] The 0.6-kb DNA fragment containing a partial p30 gene cloned had an open reading frame (ORF) of 579 bp encoding a 193-amino-acid protein with a molecular mass of 21,175 Da. The partial P30 protein of E. canis was encoded by nucleotide 97 through nucleotide 672 of the sequence shown in FIG. 19A and comprised amino acid 33 through amino acid 224 of the sequence shown in FIG. 19B.

[0100] Polynucleotides which Encode OMP 1A, OMP-1B, OMP-1C, OMP-1D, OMP-1F. and OMP1-E

[0101] A. Southern Blot Analysis.

[0102] Genomic DNA extracted from the purified E. chaffeensis (200 ng each) was digested with restriction endonucleases, electrophoresed, and transferred to Hybond-N⁺ nylon membrane (Amersham, Arlington Heights, Ill.), by a standard method. The 0.8-kb p28 gene fragment from the clone pCRIIp28 was labeled with [α−³²P]dATP by the random primer method using a kit (Boehringer Mannheim, Indianapolis, Ind.) and the labeled fragment was used as a DNA probe. Hybridization was performed at 60° C. in rapid hybridization buffer (Amersham) for 20 h. The nylon sheet was washed in 0.1×SSC (1×SSC containing 0.15M sodium chloride and 0.015M sodium citrate) with 1% SDS at 55° C. and the hybridized probes were exposed to Hyperfilm (Amersham) at −80° C.

[0103] Genomic Southern blot analysis with several restriction enzymes resulted in one or more DNA fragment(s) of E. chaffeensis which hybridized to ³²P-labeled omp-1 gene probe. The restriction enzymes used did not cut within the p28 gene portion of the pCRIIp28 insert. Xba I, BgI II, and Kpn I produced two bands, Spe I generated three bands, and EcoR V and Pst I produced multiple bands with different densities. EcoR I generated a broad band of 2.5 to 4 kb. These homologous genes are designated as omp-1 (outer membrane protein-1) family.

[0104] B. Cloning and sequencing of genomic copies of E. chaffeensis omp-1 gene.

[0105] The EcoR I and Pst I fragments of DNA, detected by genomic Southern blot analysis as described above, were inserted into pBluescript 11 KS (+) vectors, and the recombinant plasmids were introduced into E. coli DH5α. Using the colony hybridization method with the ³²P-labeled omp-1gene probe, four positive clones were isolated from the transformnant. The positive clones were designated pEC2.6; pEC3.6, pPS2.6, and pPS3.6. These contained the ehrlichial DNA fragments of 2.6-kb (EcoR I), 3.6 kb (EcoR I), 2.6 kb (Pst I), and 3.6 kb (Pst I), respectively. The inserts of the clones pEC3.6 and pPS2.6 overlapped as shown in FIG. 2. The overlapping area was further confirmed by PCR of E. chaffeensis genomic DNA with two pairs of primer sets interposing the junctions of the four clones. The 1.1- to 1.6-kb DNA fragments of HindIII-HindIII, HindIII-EcoRI, or XhoI-EcoRI in the pEC2.6 and pEC3.6 were subcloned for sequencing. DNA sequencing was performed with suitable synthetic primers by dideoxy-termination method as described above.

[0106] Four DNA fragments from 2.6 to 3.6 kb were cloned from the EcoRI-digested and the PstI-digested genomic DNA of E. chaffeensis by colony hybridization with radiolabeled omp-1 gene probe. The inserted DNA of the two recombinant clones, pEC3.6 and PPS2.6, were overlapped. Sequencing revealed one 5′-truncated ORF of 243 bp (designated omp-1A) and five complete ORF of 836-861 bp (designated omp-1B to omp-1F), which are tandemly-arrayed and are homologous to the p28 gene (but are not identical), in the ehrlichial genomic DNA of 6,292 bp. The intergenic spaces were 581 bp between omp-1A and omp-1B and 260-308 bp among others. Putative promoter regions and ribosome-binding sites were identified in the noncoding regions.

[0107] C. Sequence Analysis and GenBank Accession Number.

[0108] Nucleotide sequences were analyzed with the DNASIS program (Hitachi Software Engineering Co., Ltd., Yokohama, Japan). A homology search was carried out with databases of the GenBank, Swiss Plot, PDB and PIR by using the software basic local alignment search tool in the BLAST network service (the National Center for Biotechnology Information, Bethesda, Md.). Phylogenetic analysis was performed by using the PHYLIP software package (version 3.5). An evolutional distance matrix, generated by using the Kimura formula in the PROTDIST, was used for construction of a phylogenetic tree by using the unweighted pair-group method analysis (UPGMA) (Felsenstein, J. 1989. PHYLIP-phylogeny inference package (version 3.3). Cladistics 5:164-166). The data were also examined using parsimony analysis (PROTPARS in PHYLIP). A bootstrap analysis was carried out to investigate the stability of randomly generated trees by using SEQBOOT and CONSENSE in the same package. The nucleotide sequence of the p28 gene and its gene copies has been assigned GenBank accession numbers U72291 and AF021338, respectively.

[0109] Proteins Encoded by the omp-1 Genes.

[0110] Five complete omp-1 gene copies (omp-1B to omp-1F) encode 279 to 287-amino acid proteins with molecular masses of 30,320-31,508 Da. The 25-amino acid sequence at the N-terminus of OMP-1B to OMP-1F (encoded in omp-1B to omp-1F) is predicted to be a signal peptide because three carboxyl-terminal amino acids of the signal peptides (Ser-X-Ala in OMP-1B, Leu-X-Ser for OMP-C, and Ser-X-Ser for OMP-1D and OMP-1F) are included in the preferred amino acid sequence of signal peptidase at the processing sites proposed by Oliver. The calculated molecular masses of the mature OMP-1B to OMP-1F from the predicted amino acid sequences are 28,181 Da for OMP-1B, 27,581 Da for OMP-1C, 28,747 Da for OMP-1D, 27,776 Da for OMP-1E, and 27,933 Da for OMP-1F. The estimated isoelectric points are 4.76-5.76 in the mature OMP-1B to OMP-1F. An amino acid sequence in omp-1F gene (the 80th to 94th amino acids) was identical to the N-terminal amino acid sequences of E. chaffeensis native P23 protein as determined chemically, which indicates that P23 is derived from the omp-1F gene.

[0111] Alignment of predicted amino acid sequences of the E. chaffeensis OMP-1 family and Cowdria ruminantium, revealed substitutions or deletions of one or several contiguous amino acid residues throughout the molecules. The significant differences in sequences among the aligned proteins are seen in the regions indicated SV (semivariable region) and HV (hypervariable region) 1 to 3 in FIG. 34. Computer analysis for hydropathy revealed that protein molecules predicted from all omp-1 gene copies contain alternative hydrophilic and hydrophobic motifs which are characteristic of transmembrane proteins. The HV1 and HV2 were found to locate in the hydrophilic regions.

[0112] The amino acid sequences of 5 mature proteins without signal peptides (OMP-1, and OMP-1C to OMP-1F) were similar to one another (71-83%) but the sequence of OMP-1B was dissimilar to those of the 5 proteins (45-48%). The amino acid sequences of the 5 proteins showed an intermediate degree of similarity with that of C. ruminantium MAP-1 (59-63%), but the similarity between that of the OMP-1B and the C. ruminantium MAP-1 was low (45%). These relations are shown in a phylogenetic tree which was obtained based on the amino acid sequence alignment by UPGMA method in the PHYLIP software package. Three proteins (OMP-1, OMP-1D, and OMP-1F) and two proteins (OMP-1C and OMP-1E) formed two separate clusters. The OMP-1B was located distantly from these two clusters. The C. ruminantium MAP-1 was positioned between the OMP-1B and other members in the OMP-1 family.

[0113] Preparation of a Recombinant Form of OMP-1 and P30

[0114] The 0.8-kb p28 gene from E. chaffeensis was excised from the clone pCRIIp28 by EcoRI-NotI double-digestion, ligated into EcoRI-NotI sites of a pET 29a expression vector, and amplified in Escherichia coli BL21 (DE3)pLysS (Novagen, Inc., Madison, Wis.). The clone (designated pET29p28) produced a fusion protein with a 35-amino acid sequence carried from the vector at the N terminus. The amino acid sequence of the OMP-1 portion of the fusion protein, referred to hereinafter as rOMP-1, is depicted in FIG. 1.

[0115] An expression vector comprising the p30 gene was used to prepare the recombinant form of P30. To prepare the expression vector, an 0.6-kb fragment was excised from the clone pCRIIp30 by EcoRI digestion, ligated into EcoRI site of a pET29a expression vector, and amplifed in E. coli BL21(DE3)pLys (Novagen, Inc., Madison, Wis.). The clone (designated pET29p30) produced a fusion protein with a 35-amino-acid sequence and a 21-amino-acid sequence carried from the vector at the N and C termini, respectively. The fusion protein had an amino acid sequence consisting of 249-amino acid residues with a molecular mass of 27,316 Da. The amino acid sequence of the P30 portion of the fusion protein, referred to hereinafter as rP30, is amino acid 33 through amino acid 224 of the sequence shown in FIG. 19B.

[0116] Preparation of Anti-rOMP1 Antibody

[0117] An rOMP-1antigen was prepared by excising the gel band corresponding to the rOMP-1 protein in SDS-PAGE, mincing the band in phosphate-buffered saline (PBS), pH 7.4, and mixing with an equal volume of Freund's incomplete adjuvant (Sigma). The rOMP-i mixture (1 mg of protein each time) was subcutaneously injected into a rabbit every 2 weeks four times. A serum sample was collected from the rabbit to provide the anti-rOMP-1 antibody

[0118] The anti-rOMP-1 antibody was examined by western immunoblot analysis. The results indicated that the rabbit anti-rOMP-1 antibody recognized not only rOMP-1 (31 kDa) and OMP-1 protein, but also P29 and P25 of E. chaffeensis and P30 of E. canis. These results indicate that OMP-1 shares antigenic epitopes with P25 and P29 in E. chaffeensis and P30 of E. canis.

[0119] The following examples are for purposes of illustration only and are not intended to limit the scope of the claims which are appended hereto.

EXAMPLE 1

[0120] Assaying for the Presence of Anti-OMP-1 Antibody in a Patient

[0121] Convalescent-phase serum from a patient with clinical signs of human ehrlichiosis was used. Western blot analyses using the rP28 protein as antigen was performed with 1:1,000 dilutions of this serum. Alkaline phosphatase-conjugated affinity-purified anti-human immunoglobulin G (Kirkegaard & Perry Laboratories, Inc., Gaithersburg, Md.) was used at a 1:1,000 or 1:2,000 dilution as secondary antibodies. Results indicated that serum from a patient with clinical signs of human ehrlichiosis reacted strongly to rOMP-1 protein (31 kDa).

EXAMPLE 2

[0122] Assaying for the Presence of Anti-OMP-1 Antibody in a Patient

[0123] Convalescent-phase serum from a patient with clinical signs of human ehrlichiosis was reacted with the rP30 protein of E. canis as described in Example 1. The serum reacted strongly to rP30. These results indicate the rP30 is useful for diagnosing an infection with E. chaffeensis in human patients.

EXAMPLE 3

[0124] Identifying E. chaffeensis-Infected Cells using Anti-rOMP-1 Antibody

[0125]E. chaffeensis-infected DH82 cells were sonicated and centrifuged at 400×g for 10 min. The supernatant was then centrifuged at 10,000×g for 10 min to obtain ehrlichia-enriched pellet. The pellet was resuspended and incubated with rabbit anti-rOMP-1 antibody or normal rabbit serum (1:100 dilution) at 37° C. for 1 h in PBS containing 1% bovine serum albumin (BSA-PBS). After washing, the ehrlichiae was incubated with gold-conjugated protein G (20 nm), Sigma) at 1:30 dilution for 1 h at room temperature in BSA-PBS. After washing again, the specimen was fixed with 1.25% formaldehyde, 2.5% glutaraldehyde, and 0.03% trinitrophenol in 0.1 M cacodylate buffer (pH 7.4) for 24 h and postfixed in 1% osmium-1.5% potassium ferricyanide for 1 h (34). The section was then embedded in PolyBed 812 (Polysciences, Warraington, Pa). The specimen was ultrathin sectioned at 60 nm, stained with uranyl acetate and lead citrate, and observed with a Philips 300 transmission electron microscope at 60 kV.

[0126] Transmission immunoelectron microscopy with colloidal gold-conjugated protein G and rabbit anti-rP28 antibody revealed gold particles bound to E. chaffeensis surface. The distribution of the particles was random, close to the surface, and appeared as if almost embedded in the membrane, suggesting that the antigenic epitope protrudes very little from the lipid bilayer. Nonetheless, the antigenic epitope was surface-exposed, and thus, could be recognized by rabbit anti-rOMP-1 antibody. No gold particles were observed on host cytoplasmic membrane or E. chaffeensis incubated with normal rabbit serum.

EXAMPLE 4

[0127] Immunization of Mice and E. chaffeensis Challenge

[0128] The rOMP-1band in SDS- PAGE was excised, minced, and mixed with an equal volume of Freund's incomplete or complete adjuvant. Nine BALB/c male mice (6 weeks old) were divided into two groups. Five mice were intraperitoneally immunized a total of four times at 10-day intervals; twice with a mixture of the minced gel with the rOMP-1 (30 to 40 μg of protein per mouse each time) and incomplete adjuvant, and twice with a mixture of the recombinant protein (the same amount as before) and complete adjuvant. Four mice were intraperitoneally injected with a mixture of the minced gel without protein and the respective adjuvants. For ehrlichia-challenge, approximately 1×10⁷ DH82 cells heavily-infected with E. chaffeensis were disrupted by sonication in serum-free DMEM (GIBCO-BRL) and centrifuged at 200×g for 5 min. The supernatant was diluted to a final volume of 5 ml, and 0.3 ml was inoculated intraperitoneally into each mouse 10 days after the last immunization. Before challenge, all 5-immunized mice had a titer of 1:160 against E. chaffeensis antigen by IFA and all 4-nonimmunized mice were negative.

[0129] At day 5 post-challenge, approximately 1 ml of blood was collected in an EDTA tube from each mouse and protection was assessed by PCR detection of E. chaffeensis 16S rDNA in the buffy coat of the collected blood. E. chaffeensis could not be reisolated in cell culture at day 10 postinfection. Day 5 post challenge is the optimum time at which establishment of ehrlichial infection can be examined by PCR without the influence of residual DNA from the ehrlichiae used as the challenge before the spontaneous clearance of organisms take place. The E. chaffeensis-specific DNA fragment was observed in all nonirnmunized mice but not in any immunized mice, indicating that immunization of rOMP-1 apparently protects mice from ehrlichial infection and indicating that the OMP-1 is a potential protective antigen.

EXAMPLE 5

[0130] Assaying for the Presence of Anti-P30 Antibody in Dogs

[0131] The rP30 protein was used as an antigen in a Western immunoblot analysis and dot blot analysis to detect the presence of antibody to E. canis in serum from E. canis infected dogs. The results of the Western immunoblot analysis indicated that reactivity of the sera with rP30 was stronger than the reactivity that was observed when purified E. canis was used as antigen. The results of the dot blot assay indicated that rP30 is a useful and sensitive tool for serodiagnosis of canine ehrlichiosis.

1 66 1 846 DNA Ehrlichia chaffeensis CDS (1)..(846) 1 atg aat tac aaa aaa gtt ttc ata aca agt gca ttg ata tca tta ata 48 Met Asn Tyr Lys Lys Val Phe Ile Thr Ser Ala Leu Ile Ser Leu Ile 1 5 10 15 tct tct cta cct gga gta tca ttt tcc gac cca gca ggt agt ggt att 96 Ser Ser Leu Pro Gly Val Ser Phe Ser Asp Pro Ala Gly Ser Gly Ile 20 25 30 aac ggt aat ttc tac atc agt gga aaa tac atg cca agt gct tcg cat 144 Asn Gly Asn Phe Tyr Ile Ser Gly Lys Tyr Met Pro Ser Ala Ser His 35 40 45 ttt gga gta ttc tct gct aag gaa gaa aga aat aca aca gtt gga gtg 192 Phe Gly Val Phe Ser Ala Lys Glu Glu Arg Asn Thr Thr Val Gly Val 50 55 60 ttt gga ctg aag caa aat tgg gac gga agc gca ata tcc aac tcc tcc 240 Phe Gly Leu Lys Gln Asn Trp Asp Gly Ser Ala Ile Ser Asn Ser Ser 65 70 75 80 cca aac gat gta ttc act gtc tca aat tat tca ttt aaa tat gaa aac 288 Pro Asn Asp Val Phe Thr Val Ser Asn Tyr Ser Phe Lys Tyr Glu Asn 85 90 95 aac ccg ttt tta ggt ttt gca gga gct att ggt tac tca atg gat ggt 336 Asn Pro Phe Leu Gly Phe Ala Gly Ala Ile Gly Tyr Ser Met Asp Gly 100 105 110 cca aga ata gag ctt gaa gta tct tat gaa aca ttt gat gta aaa aat 384 Pro Arg Ile Glu Leu Glu Val Ser Tyr Glu Thr Phe Asp Val Lys Asn 115 120 125 caa ggt aac aat tat aag aat gaa gca cat aga tat tgt gct cta tcc 432 Gln Gly Asn Asn Tyr Lys Asn Glu Ala His Arg Tyr Cys Ala Leu Ser 130 135 140 cat aac tca gca gca gac atg agt agt gca agt aat aat ttt gtc ttt 480 His Asn Ser Ala Ala Asp Met Ser Ser Ala Ser Asn Asn Phe Val Phe 145 150 155 160 cta aaa aat gaa gga tta ctt gac ata tca ttt atg ctg aac gca tgc 528 Leu Lys Asn Glu Gly Leu Leu Asp Ile Ser Phe Met Leu Asn Ala Cys 165 170 175 tat gac gta gta ggc gaa ggc ata cct ttt tct cct tat ata tgc gca 576 Tyr Asp Val Val Gly Glu Gly Ile Pro Phe Ser Pro Tyr Ile Cys Ala 180 185 190 ggt atc ggt act gat tta gta tcc atg ttt gaa gct aca aat cct aaa 624 Gly Ile Gly Thr Asp Leu Val Ser Met Phe Glu Ala Thr Asn Pro Lys 195 200 205 att tct tac caa gga aag tta ggt tta agc tac tct ata agc cca gaa 672 Ile Ser Tyr Gln Gly Lys Leu Gly Leu Ser Tyr Ser Ile Ser Pro Glu 210 215 220 gct tct gtg ttt att ggt ggg cac ttt cat aag gta tta ggg aac gaa 720 Ala Ser Val Phe Ile Gly Gly His Phe His Lys Val Leu Gly Asn Glu 225 230 235 240 ttt aga gat att cct act ata ata cct act gga tca aca ctt gca gga 768 Phe Arg Asp Ile Pro Thr Ile Ile Pro Thr Gly Ser Thr Leu Ala Gly 245 250 255 aaa gga aac tac cct gca ata gta ata ctg gat gta tgc cac ttt gga 816 Lys Gly Asn Tyr Pro Ala Ile Val Ile Leu Asp Val Cys His Phe Gly 260 265 270 ata gaa ctt gga gga agg ttt gct ttc taa 846 Ile Glu Leu Gly Gly Arg Phe Ala Phe 275 280 2 281 PRT Ehrlichia chaffeensis 2 Met Asn Tyr Lys Lys Val Phe Ile Thr Ser Ala Leu Ile Ser Leu Ile 1 5 10 15 Ser Ser Leu Pro Gly Val Ser Phe Ser Asp Pro Ala Gly Ser Gly Ile 20 25 30 Asn Gly Asn Phe Tyr Ile Ser Gly Lys Tyr Met Pro Ser Ala Ser His 35 40 45 Phe Gly Val Phe Ser Ala Lys Glu Glu Arg Asn Thr Thr Val Gly Val 50 55 60 Phe Gly Leu Lys Gln Asn Trp Asp Gly Ser Ala Ile Ser Asn Ser Ser 65 70 75 80 Pro Asn Asp Val Phe Thr Val Ser Asn Tyr Ser Phe Lys Tyr Glu Asn 85 90 95 Asn Pro Phe Leu Gly Phe Ala Gly Ala Ile Gly Tyr Ser Met Asp Gly 100 105 110 Pro Arg Ile Glu Leu Glu Val Ser Tyr Glu Thr Phe Asp Val Lys Asn 115 120 125 Gln Gly Asn Asn Tyr Lys Asn Glu Ala His Arg Tyr Cys Ala Leu Ser 130 135 140 His Asn Ser Ala Ala Asp Met Ser Ser Ala Ser Asn Asn Phe Val Phe 145 150 155 160 Leu Lys Asn Glu Gly Leu Leu Asp Ile Ser Phe Met Leu Asn Ala Cys 165 170 175 Tyr Asp Val Val Gly Glu Gly Ile Pro Phe Ser Pro Tyr Ile Cys Ala 180 185 190 Gly Ile Gly Thr Asp Leu Val Ser Met Phe Glu Ala Thr Asn Pro Lys 195 200 205 Ile Ser Tyr Gln Gly Lys Leu Gly Leu Ser Tyr Ser Ile Ser Pro Glu 210 215 220 Ala Ser Val Phe Ile Gly Gly His Phe His Lys Val Leu Gly Asn Glu 225 230 235 240 Phe Arg Asp Ile Pro Thr Ile Ile Pro Thr Gly Ser Thr Leu Ala Gly 245 250 255 Lys Gly Asn Tyr Pro Ala Ile Val Ile Leu Asp Val Cys His Phe Gly 260 265 270 Ile Glu Leu Gly Gly Arg Phe Ala Phe 275 280 3 852 DNA Ehrlichia chaffeensis CDS (1)..(852) 3 atg aat tac aag aaa att ttt gta agc agt gca tta att tca tta atg 48 Met Asn Tyr Lys Lys Ile Phe Val Ser Ser Ala Leu Ile Ser Leu Met 1 5 10 15 tca atc tta cct tac caa tct ttt gca gat cct gta act tca aat gat 96 Ser Ile Leu Pro Tyr Gln Ser Phe Ala Asp Pro Val Thr Ser Asn Asp 20 25 30 aca gga atc aac gac agc aga gaa ggc ttc tac att agt gta aag tat 144 Thr Gly Ile Asn Asp Ser Arg Glu Gly Phe Tyr Ile Ser Val Lys Tyr 35 40 45 aat cca agc ata tca cac ttc aga aaa ttc tca gct gaa gaa gct ccc 192 Asn Pro Ser Ile Ser His Phe Arg Lys Phe Ser Ala Glu Glu Ala Pro 50 55 60 atc aat gga aat act tct atc act aaa aag gtt ttc ggg ctg aaa aaa 240 Ile Asn Gly Asn Thr Ser Ile Thr Lys Lys Val Phe Gly Leu Lys Lys 65 70 75 80 gac gga gat ata gca caa tct gcg aat ttt aac agg aca gat cca gcc 288 Asp Gly Asp Ile Ala Gln Ser Ala Asn Phe Asn Arg Thr Asp Pro Ala 85 90 95 ctc gag ttt cag aat aac cta ata tca gga ttc tca gga agt att ggt 336 Leu Glu Phe Gln Asn Asn Leu Ile Ser Gly Phe Ser Gly Ser Ile Gly 100 105 110 tat gct atg gat ggg cca aga ata gaa ctt gaa gct gca tac caa aaa 384 Tyr Ala Met Asp Gly Pro Arg Ile Glu Leu Glu Ala Ala Tyr Gln Lys 115 120 125 ttt gat gca aaa aat cct gac aac aat gac act aat agc ggt gac tac 432 Phe Asp Ala Lys Asn Pro Asp Asn Asn Asp Thr Asn Ser Gly Asp Tyr 130 135 140 tat aaa tac ttt gga cta tct cgt gaa gac gca ata gca gat aag aaa 480 Tyr Lys Tyr Phe Gly Leu Ser Arg Glu Asp Ala Ile Ala Asp Lys Lys 145 150 155 160 tat gtt gtc ctt aaa aat gaa ggc atc act ttt atg tca tta atg gtt 528 Tyr Val Val Leu Lys Asn Glu Gly Ile Thr Phe Met Ser Leu Met Val 165 170 175 aac act tgc tat gac att aca gct gaa gga gta cct ttc ata ccg tat 576 Asn Thr Cys Tyr Asp Ile Thr Ala Glu Gly Val Pro Phe Ile Pro Tyr 180 185 190 gca tgt gca ggt gta gga gca gac ctt ata aac gta ttt aag gat ttt 624 Ala Cys Ala Gly Val Gly Ala Asp Leu Ile Asn Val Phe Lys Asp Phe 195 200 205 aat tta aaa ttc tca tac caa ggg aaa ata ggt att agc tat cca atc 672 Asn Leu Lys Phe Ser Tyr Gln Gly Lys Ile Gly Ile Ser Tyr Pro Ile 210 215 220 aca cca gaa gtt tcc gct ttt att gga gga tac tac cac gga gtt ata 720 Thr Pro Glu Val Ser Ala Phe Ile Gly Gly Tyr Tyr His Gly Val Ile 225 230 235 240 gga aat aat ttt aac aaa ata cct gta ata aca cct gta gta tta gaa 768 Gly Asn Asn Phe Asn Lys Ile Pro Val Ile Thr Pro Val Val Leu Glu 245 250 255 gga gct cct caa aca aca tct gcg cta gta act att gac act gga tac 816 Gly Ala Pro Gln Thr Thr Ser Ala Leu Val Thr Ile Asp Thr Gly Tyr 260 265 270 ttt ggc gga gaa gtt gga gta agg ttc acc ttc tag 852 Phe Gly Gly Glu Val Gly Val Arg Phe Thr Phe 275 280 4 283 PRT Ehrlichia chaffeensis 4 Met Asn Tyr Lys Lys Ile Phe Val Ser Ser Ala Leu Ile Ser Leu Met 1 5 10 15 Ser Ile Leu Pro Tyr Gln Ser Phe Ala Asp Pro Val Thr Ser Asn Asp 20 25 30 Thr Gly Ile Asn Asp Ser Arg Glu Gly Phe Tyr Ile Ser Val Lys Tyr 35 40 45 Asn Pro Ser Ile Ser His Phe Arg Lys Phe Ser Ala Glu Glu Ala Pro 50 55 60 Ile Asn Gly Asn Thr Ser Ile Thr Lys Lys Val Phe Gly Leu Lys Lys 65 70 75 80 Asp Gly Asp Ile Ala Gln Ser Ala Asn Phe Asn Arg Thr Asp Pro Ala 85 90 95 Leu Glu Phe Gln Asn Asn Leu Ile Ser Gly Phe Ser Gly Ser Ile Gly 100 105 110 Tyr Ala Met Asp Gly Pro Arg Ile Glu Leu Glu Ala Ala Tyr Gln Lys 115 120 125 Phe Asp Ala Lys Asn Pro Asp Asn Asn Asp Thr Asn Ser Gly Asp Tyr 130 135 140 Tyr Lys Tyr Phe Gly Leu Ser Arg Glu Asp Ala Ile Ala Asp Lys Lys 145 150 155 160 Tyr Val Val Leu Lys Asn Glu Gly Ile Thr Phe Met Ser Leu Met Val 165 170 175 Asn Thr Cys Tyr Asp Ile Thr Ala Glu Gly Val Pro Phe Ile Pro Tyr 180 185 190 Ala Cys Ala Gly Val Gly Ala Asp Leu Ile Asn Val Phe Lys Asp Phe 195 200 205 Asn Leu Lys Phe Ser Tyr Gln Gly Lys Ile Gly Ile Ser Tyr Pro Ile 210 215 220 Thr Pro Glu Val Ser Ala Phe Ile Gly Gly Tyr Tyr His Gly Val Ile 225 230 235 240 Gly Asn Asn Phe Asn Lys Ile Pro Val Ile Thr Pro Val Val Leu Glu 245 250 255 Gly Ala Pro Gln Thr Thr Ser Ala Leu Val Thr Ile Asp Thr Gly Tyr 260 265 270 Phe Gly Gly Glu Val Gly Val Arg Phe Thr Phe 275 280 5 843 DNA Ehrlichia chaffeensis CDS (1)..(843) 5 atg aac tgc aaa aaa ttt ttt ata aca act gca ttg gca ttg cca atg 48 Met Asn Cys Lys Lys Phe Phe Ile Thr Thr Ala Leu Ala Leu Pro Met 1 5 10 15 tct ttc tta cct gga ata tta ctt tct gaa cca gta caa gat gac agt 96 Ser Phe Leu Pro Gly Ile Leu Leu Ser Glu Pro Val Gln Asp Asp Ser 20 25 30 gtg agt ggc aat ttc tat att agt ggc aag tac atg cca agt gct tct 144 Val Ser Gly Asn Phe Tyr Ile Ser Gly Lys Tyr Met Pro Ser Ala Ser 35 40 45 cat ttt gga gtt ttc tct gcc aaa gaa gaa aaa aat cct act gtc gcg 192 His Phe Gly Val Phe Ser Ala Lys Glu Glu Lys Asn Pro Thr Val Ala 50 55 60 ttg tat ggt ttg aaa caa gat tgg aac ggt gtt agt gct tca agt cat 240 Leu Tyr Gly Leu Lys Gln Asp Trp Asn Gly Val Ser Ala Ser Ser His 65 70 75 80 gct gat gcg gac ttt aat aac aaa ggt tat tct ttt aaa tac gaa aac 288 Ala Asp Ala Asp Phe Asn Asn Lys Gly Tyr Ser Phe Lys Tyr Glu Asn 85 90 95 aat cca ttt cta ggt ttt gca gga gct att ggt tat tca atg ggt ggt 336 Asn Pro Phe Leu Gly Phe Ala Gly Ala Ile Gly Tyr Ser Met Gly Gly 100 105 110 cca aga ata gag ttt gaa gtg tcc tat gaa aca ttt gac gtg aaa aat 384 Pro Arg Ile Glu Phe Glu Val Ser Tyr Glu Thr Phe Asp Val Lys Asn 115 120 125 caa ggt ggt aat tac aaa aat gat gct cac aga tac tgt gcc tta gat 432 Gln Gly Gly Asn Tyr Lys Asn Asp Ala His Arg Tyr Cys Ala Leu Asp 130 135 140 cgt aaa gca agc agc act aat gcc aca gct agt cac tac gtg cta cta 480 Arg Lys Ala Ser Ser Thr Asn Ala Thr Ala Ser His Tyr Val Leu Leu 145 150 155 160 aaa aat gaa gga cta ctt gat ata tca ctt atg ttg aat gca tgc tat 528 Lys Asn Glu Gly Leu Leu Asp Ile Ser Leu Met Leu Asn Ala Cys Tyr 165 170 175 gac gta gta agt gaa gga ata cct ttc tct cct tac ata tgt gca ggt 576 Asp Val Val Ser Glu Gly Ile Pro Phe Ser Pro Tyr Ile Cys Ala Gly 180 185 190 gtt ggt acc gat tta ata tcc atg ttt gaa gct ata aac cct aaa att 624 Val Gly Thr Asp Leu Ile Ser Met Phe Glu Ala Ile Asn Pro Lys Ile 195 200 205 tct tat caa gga aag tta ggt ttg agt tac tct ata aac cca gaa gct 672 Ser Tyr Gln Gly Lys Leu Gly Leu Ser Tyr Ser Ile Asn Pro Glu Ala 210 215 220 tct gtc ttt gtt ggt gga cat ttt cat aaa gtt gca ggt aat gaa ttc 720 Ser Val Phe Val Gly Gly His Phe His Lys Val Ala Gly Asn Glu Phe 225 230 235 240 agg gac att tct act ctt aaa gcg ttt gct aca cca tca tct gca gct 768 Arg Asp Ile Ser Thr Leu Lys Ala Phe Ala Thr Pro Ser Ser Ala Ala 245 250 255 act cca gac tta gca aca gta aca ctg agt gtg tgt cac ttt gga gta 816 Thr Pro Asp Leu Ala Thr Val Thr Leu Ser Val Cys His Phe Gly Val 260 265 270 gaa ctt gga gga aga ttt aac ttc taa 843 Glu Leu Gly Gly Arg Phe Asn Phe 275 280 6 280 PRT Ehrlichia chaffeensis 6 Met Asn Cys Lys Lys Phe Phe Ile Thr Thr Ala Leu Ala Leu Pro Met 1 5 10 15 Ser Phe Leu Pro Gly Ile Leu Leu Ser Glu Pro Val Gln Asp Asp Ser 20 25 30 Val Ser Gly Asn Phe Tyr Ile Ser Gly Lys Tyr Met Pro Ser Ala Ser 35 40 45 His Phe Gly Val Phe Ser Ala Lys Glu Glu Lys Asn Pro Thr Val Ala 50 55 60 Leu Tyr Gly Leu Lys Gln Asp Trp Asn Gly Val Ser Ala Ser Ser His 65 70 75 80 Ala Asp Ala Asp Phe Asn Asn Lys Gly Tyr Ser Phe Lys Tyr Glu Asn 85 90 95 Asn Pro Phe Leu Gly Phe Ala Gly Ala Ile Gly Tyr Ser Met Gly Gly 100 105 110 Pro Arg Ile Glu Phe Glu Val Ser Tyr Glu Thr Phe Asp Val Lys Asn 115 120 125 Gln Gly Gly Asn Tyr Lys Asn Asp Ala His Arg Tyr Cys Ala Leu Asp 130 135 140 Arg Lys Ala Ser Ser Thr Asn Ala Thr Ala Ser His Tyr Val Leu Leu 145 150 155 160 Lys Asn Glu Gly Leu Leu Asp Ile Ser Leu Met Leu Asn Ala Cys Tyr 165 170 175 Asp Val Val Ser Glu Gly Ile Pro Phe Ser Pro Tyr Ile Cys Ala Gly 180 185 190 Val Gly Thr Asp Leu Ile Ser Met Phe Glu Ala Ile Asn Pro Lys Ile 195 200 205 Ser Tyr Gln Gly Lys Leu Gly Leu Ser Tyr Ser Ile Asn Pro Glu Ala 210 215 220 Ser Val Phe Val Gly Gly His Phe His Lys Val Ala Gly Asn Glu Phe 225 230 235 240 Arg Asp Ile Ser Thr Leu Lys Ala Phe Ala Thr Pro Ser Ser Ala Ala 245 250 255 Thr Pro Asp Leu Ala Thr Val Thr Leu Ser Val Cys His Phe Gly Val 260 265 270 Glu Leu Gly Gly Arg Phe Asn Phe 275 280 7 861 DNA Ehrlichia chaffeensis CDS (1)..(861) 7 atg aac tgc gaa aaa ttt ttt ata aca act gca tta aca tta cta atg 48 Met Asn Cys Glu Lys Phe Phe Ile Thr Thr Ala Leu Thr Leu Leu Met 1 5 10 15 tcc ttc tta cct gga ata tca ctt tct gat cca gta cag gat gac aac 96 Ser Phe Leu Pro Gly Ile Ser Leu Ser Asp Pro Val Gln Asp Asp Asn 20 25 30 att agt ggt aat ttc tac atc agt gga aag tat atg cca agc gct tcg 144 Ile Ser Gly Asn Phe Tyr Ile Ser Gly Lys Tyr Met Pro Ser Ala Ser 35 40 45 cat ttt gga gtt ttt tct gcc aag gaa gaa aga aat aca aca gtt gga 192 His Phe Gly Val Phe Ser Ala Lys Glu Glu Arg Asn Thr Thr Val Gly 50 55 60 gta ttt gga ata gag caa gat tgg gat aga tgt gta ata tct aga acc 240 Val Phe Gly Ile Glu Gln Asp Trp Asp Arg Cys Val Ile Ser Arg Thr 65 70 75 80 act tta agc gat ata ttc acc gtt cca aat tat tca ttt aag tat gaa 288 Thr Leu Ser Asp Ile Phe Thr Val Pro Asn Tyr Ser Phe Lys Tyr Glu 85 90 95 aat aat cta ttt tca gga ttt gca gga gct att ggc tac tca atg gat 336 Asn Asn Leu Phe Ser Gly Phe Ala Gly Ala Ile Gly Tyr Ser Met Asp 100 105 110 ggc cca aga ata gag ctt gaa gta tct tat gaa gca ttc gat gtt aaa 384 Gly Pro Arg Ile Glu Leu Glu Val Ser Tyr Glu Ala Phe Asp Val Lys 115 120 125 aat caa ggt aac aat tat aag aac gaa gca cat aga tat tat gct ctg 432 Asn Gln Gly Asn Asn Tyr Lys Asn Glu Ala His Arg Tyr Tyr Ala Leu 130 135 140 tcc cat ctt ctc ggc aca gag aca cag ata gat ggt gca ggc agt gcg 480 Ser His Leu Leu Gly Thr Glu Thr Gln Ile Asp Gly Ala Gly Ser Ala 145 150 155 160 tct gtc ttt cta ata aat gaa gga cta ctt gat aaa tca ttt atg ctg 528 Ser Val Phe Leu Ile Asn Glu Gly Leu Leu Asp Lys Ser Phe Met Leu 165 170 175 aac gca tgt tat gat gta ata agt gaa ggc ata cct ttt tct cct tat 576 Asn Ala Cys Tyr Asp Val Ile Ser Glu Gly Ile Pro Phe Ser Pro Tyr 180 185 190 ata tgt gca ggt att ggt att gat tta gta tcc atg ttt gaa gct ata 624 Ile Cys Ala Gly Ile Gly Ile Asp Leu Val Ser Met Phe Glu Ala Ile 195 200 205 aat cct aaa att tct tat caa gga aaa tta ggc tta agt tac cct ata 672 Asn Pro Lys Ile Ser Tyr Gln Gly Lys Leu Gly Leu Ser Tyr Pro Ile 210 215 220 agc cca gaa gct tct gtg ttt att ggt gga cat ttt cat aag gtg ata 720 Ser Pro Glu Ala Ser Val Phe Ile Gly Gly His Phe His Lys Val Ile 225 230 235 240 gga aac gaa ttt aga gat att cct act atg ata cct agt gaa tca gcg 768 Gly Asn Glu Phe Arg Asp Ile Pro Thr Met Ile Pro Ser Glu Ser Ala 245 250 255 ctt gca gga aaa gga aac tac cct gca ata gta aca ctg gac gtg ttc 816 Leu Ala Gly Lys Gly Asn Tyr Pro Ala Ile Val Thr Leu Asp Val Phe 260 265 270 tac ttt ggc ata gaa ctt gga gga agg ttt aac ttc caa ctt tga 861 Tyr Phe Gly Ile Glu Leu Gly Gly Arg Phe Asn Phe Gln Leu 275 280 285 8 286 PRT Ehrlichia chaffeensis 8 Met Asn Cys Glu Lys Phe Phe Ile Thr Thr Ala Leu Thr Leu Leu Met 1 5 10 15 Ser Phe Leu Pro Gly Ile Ser Leu Ser Asp Pro Val Gln Asp Asp Asn 20 25 30 Ile Ser Gly Asn Phe Tyr Ile Ser Gly Lys Tyr Met Pro Ser Ala Ser 35 40 45 His Phe Gly Val Phe Ser Ala Lys Glu Glu Arg Asn Thr Thr Val Gly 50 55 60 Val Phe Gly Ile Glu Gln Asp Trp Asp Arg Cys Val Ile Ser Arg Thr 65 70 75 80 Thr Leu Ser Asp Ile Phe Thr Val Pro Asn Tyr Ser Phe Lys Tyr Glu 85 90 95 Asn Asn Leu Phe Ser Gly Phe Ala Gly Ala Ile Gly Tyr Ser Met Asp 100 105 110 Gly Pro Arg Ile Glu Leu Glu Val Ser Tyr Glu Ala Phe Asp Val Lys 115 120 125 Asn Gln Gly Asn Asn Tyr Lys Asn Glu Ala His Arg Tyr Tyr Ala Leu 130 135 140 Ser His Leu Leu Gly Thr Glu Thr Gln Ile Asp Gly Ala Gly Ser Ala 145 150 155 160 Ser Val Phe Leu Ile Asn Glu Gly Leu Leu Asp Lys Ser Phe Met Leu 165 170 175 Asn Ala Cys Tyr Asp Val Ile Ser Glu Gly Ile Pro Phe Ser Pro Tyr 180 185 190 Ile Cys Ala Gly Ile Gly Ile Asp Leu Val Ser Met Phe Glu Ala Ile 195 200 205 Asn Pro Lys Ile Ser Tyr Gln Gly Lys Leu Gly Leu Ser Tyr Pro Ile 210 215 220 Ser Pro Glu Ala Ser Val Phe Ile Gly Gly His Phe His Lys Val Ile 225 230 235 240 Gly Asn Glu Phe Arg Asp Ile Pro Thr Met Ile Pro Ser Glu Ser Ala 245 250 255 Leu Ala Gly Lys Gly Asn Tyr Pro Ala Ile Val Thr Leu Asp Val Phe 260 265 270 Tyr Phe Gly Ile Glu Leu Gly Gly Arg Phe Asn Phe Gln Leu 275 280 285 9 837 DNA Ehrlichia chaffeensis CDS (1)..(837) 9 atg aat tgc aaa aaa ttt ttt ata aca act gca tta gta tca cta atg 48 Met Asn Cys Lys Lys Phe Phe Ile Thr Thr Ala Leu Val Ser Leu Met 1 5 10 15 tcc ttt cta cct gga ata tca ttt tct gat cca gtg caa ggt gac aat 96 Ser Phe Leu Pro Gly Ile Ser Phe Ser Asp Pro Val Gln Gly Asp Asn 20 25 30 att agt ggt aat ttc tat gtt agt ggc aag tat atg cca agt gct tcg 144 Ile Ser Gly Asn Phe Tyr Val Ser Gly Lys Tyr Met Pro Ser Ala Ser 35 40 45 cat ttt ggc atg ttt tct gcc aaa gaa gaa aaa aat cct act gtt gca 192 His Phe Gly Met Phe Ser Ala Lys Glu Glu Lys Asn Pro Thr Val Ala 50 55 60 ttg tat ggc tta aaa caa gat tgg gaa ggg att agc tca tca agt cac 240 Leu Tyr Gly Leu Lys Gln Asp Trp Glu Gly Ile Ser Ser Ser Ser His 65 70 75 80 aat gat aat cat ttc aat aac aag ggt tat tca ttt aaa tat gaa aat 288 Asn Asp Asn His Phe Asn Asn Lys Gly Tyr Ser Phe Lys Tyr Glu Asn 85 90 95 aac cca ttt tta ggg ttt gca gga gct att ggt tat tca atg ggt ggt 336 Asn Pro Phe Leu Gly Phe Ala Gly Ala Ile Gly Tyr Ser Met Gly Gly 100 105 110 cca aga gta gag ttt gaa gtg tcc tat gaa aca ttt gac gtt aaa aat 384 Pro Arg Val Glu Phe Glu Val Ser Tyr Glu Thr Phe Asp Val Lys Asn 115 120 125 cag ggt aat aac tat aaa aat gat gct cac aga tac tgt gct tta ggt 432 Gln Gly Asn Asn Tyr Lys Asn Asp Ala His Arg Tyr Cys Ala Leu Gly 130 135 140 caa caa gac aac agc gga ata cct aaa act agt aaa tac gta ctg tta 480 Gln Gln Asp Asn Ser Gly Ile Pro Lys Thr Ser Lys Tyr Val Leu Leu 145 150 155 160 aaa agc gaa gga ttg ctt gac ata tca ttt atg cta aat gca tgc tat 528 Lys Ser Glu Gly Leu Leu Asp Ile Ser Phe Met Leu Asn Ala Cys Tyr 165 170 175 gat ata ata aac gag agc ata cct ttg tct cct tac ata tgt gca ggt 576 Asp Ile Ile Asn Glu Ser Ile Pro Leu Ser Pro Tyr Ile Cys Ala Gly 180 185 190 gtt ggt act gat tta ata tcc atg ttt gaa gct aca aat cct aaa att 624 Val Gly Thr Asp Leu Ile Ser Met Phe Glu Ala Thr Asn Pro Lys Ile 195 200 205 tct tac caa ggg aag tta ggt cta agt tac tct ata aac cca gaa gct 672 Ser Tyr Gln Gly Lys Leu Gly Leu Ser Tyr Ser Ile Asn Pro Glu Ala 210 215 220 tct gta ttt att ggt gga cat ttt cat aag gtg ata gga aac gaa ttt 720 Ser Val Phe Ile Gly Gly His Phe His Lys Val Ile Gly Asn Glu Phe 225 230 235 240 agg gac att cct act ctg aaa gca ttt gtt acg tca tca gct act cca 768 Arg Asp Ile Pro Thr Leu Lys Ala Phe Val Thr Ser Ser Ala Thr Pro 245 250 255 gat cta gca ata gta aca cta agt gta tgt cat ttt gga ata gaa ctt 816 Asp Leu Ala Ile Val Thr Leu Ser Val Cys His Phe Gly Ile Glu Leu 260 265 270 gga gga agg ttt aac ttc taa 837 Gly Gly Arg Phe Asn Phe 275 10 278 PRT Ehrlichia chaffeensis 10 Met Asn Cys Lys Lys Phe Phe Ile Thr Thr Ala Leu Val Ser Leu Met 1 5 10 15 Ser Phe Leu Pro Gly Ile Ser Phe Ser Asp Pro Val Gln Gly Asp Asn 20 25 30 Ile Ser Gly Asn Phe Tyr Val Ser Gly Lys Tyr Met Pro Ser Ala Ser 35 40 45 His Phe Gly Met Phe Ser Ala Lys Glu Glu Lys Asn Pro Thr Val Ala 50 55 60 Leu Tyr Gly Leu Lys Gln Asp Trp Glu Gly Ile Ser Ser Ser Ser His 65 70 75 80 Asn Asp Asn His Phe Asn Asn Lys Gly Tyr Ser Phe Lys Tyr Glu Asn 85 90 95 Asn Pro Phe Leu Gly Phe Ala Gly Ala Ile Gly Tyr Ser Met Gly Gly 100 105 110 Pro Arg Val Glu Phe Glu Val Ser Tyr Glu Thr Phe Asp Val Lys Asn 115 120 125 Gln Gly Asn Asn Tyr Lys Asn Asp Ala His Arg Tyr Cys Ala Leu Gly 130 135 140 Gln Gln Asp Asn Ser Gly Ile Pro Lys Thr Ser Lys Tyr Val Leu Leu 145 150 155 160 Lys Ser Glu Gly Leu Leu Asp Ile Ser Phe Met Leu Asn Ala Cys Tyr 165 170 175 Asp Ile Ile Asn Glu Ser Ile Pro Leu Ser Pro Tyr Ile Cys Ala Gly 180 185 190 Val Gly Thr Asp Leu Ile Ser Met Phe Glu Ala Thr Asn Pro Lys Ile 195 200 205 Ser Tyr Gln Gly Lys Leu Gly Leu Ser Tyr Ser Ile Asn Pro Glu Ala 210 215 220 Ser Val Phe Ile Gly Gly His Phe His Lys Val Ile Gly Asn Glu Phe 225 230 235 240 Arg Asp Ile Pro Thr Leu Lys Ala Phe Val Thr Ser Ser Ala Thr Pro 245 250 255 Asp Leu Ala Ile Val Thr Leu Ser Val Cys His Phe Gly Ile Glu Leu 260 265 270 Gly Gly Arg Phe Asn Phe 275 11 843 DNA Ehrlichia chaffeensis CDS (1)..(843) 11 atg aat tgc aaa aaa ttt ttt ata aca act aca tta gta tcg cta atg 48 Met Asn Cys Lys Lys Phe Phe Ile Thr Thr Thr Leu Val Ser Leu Met 1 5 10 15 tcc ttc tta cct gga ata tca ttt tct gat gca gta cag aac gac aat 96 Ser Phe Leu Pro Gly Ile Ser Phe Ser Asp Ala Val Gln Asn Asp Asn 20 25 30 gtt ggt ggt aat ttc tat atc agt ggg aaa tat gta cca agt gtt tca 144 Val Gly Gly Asn Phe Tyr Ile Ser Gly Lys Tyr Val Pro Ser Val Ser 35 40 45 cat ttt ggc gta ttc tct gct aaa cag gaa aga aat aca aca acc gga 192 His Phe Gly Val Phe Ser Ala Lys Gln Glu Arg Asn Thr Thr Thr Gly 50 55 60 gta ttt gga tta aag caa gat tgg gat ggc agc aca ata tct aaa aat 240 Val Phe Gly Leu Lys Gln Asp Trp Asp Gly Ser Thr Ile Ser Lys Asn 65 70 75 80 tct cca gaa aat aca ttt aac gtt cca aat tat tca ttt aaa tat gaa 288 Ser Pro Glu Asn Thr Phe Asn Val Pro Asn Tyr Ser Phe Lys Tyr Glu 85 90 95 aat aat cca ttt cta ggt ttt gca gga gct gtt ggt tat tta atg aat 336 Asn Asn Pro Phe Leu Gly Phe Ala Gly Ala Val Gly Tyr Leu Met Asn 100 105 110 ggt cca aga ata gag tta gaa atg tcc tat gaa aca ttt gat gtg aaa 384 Gly Pro Arg Ile Glu Leu Glu Met Ser Tyr Glu Thr Phe Asp Val Lys 115 120 125 aac cag ggt aat aac tat aag aac gat gct cac aaa tat tat gct tta 432 Asn Gln Gly Asn Asn Tyr Lys Asn Asp Ala His Lys Tyr Tyr Ala Leu 130 135 140 acc cat aac agt ggg gga aag cta agc aat gca ggt gat aag ttt gtt 480 Thr His Asn Ser Gly Gly Lys Leu Ser Asn Ala Gly Asp Lys Phe Val 145 150 155 160 ttt cta aaa aat gaa gga cta ctt gat ata tca ctt atg ttg aat gca 528 Phe Leu Lys Asn Glu Gly Leu Leu Asp Ile Ser Leu Met Leu Asn Ala 165 170 175 tgc tat gat gta ata agt gaa gga ata cct ttc tct cct tac ata tgt 576 Cys Tyr Asp Val Ile Ser Glu Gly Ile Pro Phe Ser Pro Tyr Ile Cys 180 185 190 gca ggt gtt ggt act gat tta ata tcc atg ttt gaa gct ata aac cct 624 Ala Gly Val Gly Thr Asp Leu Ile Ser Met Phe Glu Ala Ile Asn Pro 195 200 205 aaa att tct tat caa gga aag tta ggt ttg agt tac tcc ata agc cca 672 Lys Ile Ser Tyr Gln Gly Lys Leu Gly Leu Ser Tyr Ser Ile Ser Pro 210 215 220 gaa gct tct gtt ttt gtt ggt gga cat ttt cat aag gtg ata ggg aat 720 Glu Ala Ser Val Phe Val Gly Gly His Phe His Lys Val Ile Gly Asn 225 230 235 240 gaa ttc aga gat att cct gct atg ata ccc agt acc tca act ctc aca 768 Glu Phe Arg Asp Ile Pro Ala Met Ile Pro Ser Thr Ser Thr Leu Thr 245 250 255 ggt aat cac ttt act ata gta aca cta agt gta tgc cac ttt gga gtg 816 Gly Asn His Phe Thr Ile Val Thr Leu Ser Val Cys His Phe Gly Val 260 265 270 gaa ctt gga gga agg ttt aac ttt taa 843 Glu Leu Gly Gly Arg Phe Asn Phe 275 280 12 280 PRT Ehrlichia chaffeensis 12 Met Asn Cys Lys Lys Phe Phe Ile Thr Thr Thr Leu Val Ser Leu Met 1 5 10 15 Ser Phe Leu Pro Gly Ile Ser Phe Ser Asp Ala Val Gln Asn Asp Asn 20 25 30 Val Gly Gly Asn Phe Tyr Ile Ser Gly Lys Tyr Val Pro Ser Val Ser 35 40 45 His Phe Gly Val Phe Ser Ala Lys Gln Glu Arg Asn Thr Thr Thr Gly 50 55 60 Val Phe Gly Leu Lys Gln Asp Trp Asp Gly Ser Thr Ile Ser Lys Asn 65 70 75 80 Ser Pro Glu Asn Thr Phe Asn Val Pro Asn Tyr Ser Phe Lys Tyr Glu 85 90 95 Asn Asn Pro Phe Leu Gly Phe Ala Gly Ala Val Gly Tyr Leu Met Asn 100 105 110 Gly Pro Arg Ile Glu Leu Glu Met Ser Tyr Glu Thr Phe Asp Val Lys 115 120 125 Asn Gln Gly Asn Asn Tyr Lys Asn Asp Ala His Lys Tyr Tyr Ala Leu 130 135 140 Thr His Asn Ser Gly Gly Lys Leu Ser Asn Ala Gly Asp Lys Phe Val 145 150 155 160 Phe Leu Lys Asn Glu Gly Leu Leu Asp Ile Ser Leu Met Leu Asn Ala 165 170 175 Cys Tyr Asp Val Ile Ser Glu Gly Ile Pro Phe Ser Pro Tyr Ile Cys 180 185 190 Ala Gly Val Gly Thr Asp Leu Ile Ser Met Phe Glu Ala Ile Asn Pro 195 200 205 Lys Ile Ser Tyr Gln Gly Lys Leu Gly Leu Ser Tyr Ser Ile Ser Pro 210 215 220 Glu Ala Ser Val Phe Val Gly Gly His Phe His Lys Val Ile Gly Asn 225 230 235 240 Glu Phe Arg Asp Ile Pro Ala Met Ile Pro Ser Thr Ser Thr Leu Thr 245 250 255 Gly Asn His Phe Thr Ile Val Thr Leu Ser Val Cys His Phe Gly Val 260 265 270 Glu Leu Gly Gly Arg Phe Asn Phe 275 280 13 894 DNA Ehrlichia chaffeensis CDS (1)..(894) 13 atg gaa aat ctc atg aat aag aaa aac aaa ttc ttt aca ata agt aca 48 Met Glu Asn Leu Met Asn Lys Lys Asn Lys Phe Phe Thr Ile Ser Thr 1 5 10 15 gca atg gta tgc tta ttg tta tta cct ggt ata tca ttt tca gaa act 96 Ala Met Val Cys Leu Leu Leu Leu Pro Gly Ile Ser Phe Ser Glu Thr 20 25 30 ata aac aac agt gct aaa aaa cag cct ggg tta tat atc agt ggg cag 144 Ile Asn Asn Ser Ala Lys Lys Gln Pro Gly Leu Tyr Ile Ser Gly Gln 35 40 45 tac aaa cct agt gtt tca gtt ttt agt aat ttt tca gta aaa gaa act 192 Tyr Lys Pro Ser Val Ser Val Phe Ser Asn Phe Ser Val Lys Glu Thr 50 55 60 aat gtt ccc aca aag cag tta ata gca ctt aaa aaa gac att aat tct 240 Asn Val Pro Thr Lys Gln Leu Ile Ala Leu Lys Lys Asp Ile Asn Ser 65 70 75 80 gtt gca gtt ggt agt aat gct act aca ggt att agc aat cca ggt aat 288 Val Ala Val Gly Ser Asn Ala Thr Thr Gly Ile Ser Asn Pro Gly Asn 85 90 95 ttc aca att cct tat act gca gaa ttt caa gat aat gtt gcc aat ttc 336 Phe Thr Ile Pro Tyr Thr Ala Glu Phe Gln Asp Asn Val Ala Asn Phe 100 105 110 aat ggg gct gtt ggt tac tct ttt cct gat agt cta aga att gaa ata 384 Asn Gly Ala Val Gly Tyr Ser Phe Pro Asp Ser Leu Arg Ile Glu Ile 115 120 125 gag gga ttt cat gaa aaa ttt gat gtc aaa aac cct gga ggt tac aca 432 Glu Gly Phe His Glu Lys Phe Asp Val Lys Asn Pro Gly Gly Tyr Thr 130 135 140 caa gta aaa gat gcg tac cgt tat ttt gca cta gca cgt gat tta aaa 480 Gln Val Lys Asp Ala Tyr Arg Tyr Phe Ala Leu Ala Arg Asp Leu Lys 145 150 155 160 gat ggc ttc ttt gaa cct aaa gcg gaa gat aca ggt gtt tat cat act 528 Asp Gly Phe Phe Glu Pro Lys Ala Glu Asp Thr Gly Val Tyr His Thr 165 170 175 gtt atg aaa aat gat gga tta tct att tta tct act atg gtt aac gtc 576 Val Met Lys Asn Asp Gly Leu Ser Ile Leu Ser Thr Met Val Asn Val 180 185 190 tgt tac gat ttt tct gta gat gaa tta cca gtc tta cct tat ata tgt 624 Cys Tyr Asp Phe Ser Val Asp Glu Leu Pro Val Leu Pro Tyr Ile Cys 195 200 205 gca ggt atg ggt ata aac gcc ata gaa ttc ttc gac gct tta cat gta 672 Ala Gly Met Gly Ile Asn Ala Ile Glu Phe Phe Asp Ala Leu His Val 210 215 220 aaa ttt gct tac caa ggc aaa cta ggt att agc tat caa cta ttt act 720 Lys Phe Ala Tyr Gln Gly Lys Leu Gly Ile Ser Tyr Gln Leu Phe Thr 225 230 235 240 aaa gta aat tta ttc ctt gat ggg tat tac cat caa gta ata ggc aat 768 Lys Val Asn Leu Phe Leu Asp Gly Tyr Tyr His Gln Val Ile Gly Asn 245 250 255 caa ttc aaa aac tta aac gta aac cat gtt tac aca ctt aaa gaa tct 816 Gln Phe Lys Asn Leu Asn Val Asn His Val Tyr Thr Leu Lys Glu Ser 260 265 270 cct aaa gtc aca tct gca gta gct aca ctt gac att gca tac ttt ggt 864 Pro Lys Val Thr Ser Ala Val Ala Thr Leu Asp Ile Ala Tyr Phe Gly 275 280 285 ggc gaa gtt gga ata aga ttc aca ttt taa 894 Gly Glu Val Gly Ile Arg Phe Thr Phe 290 295 14 297 PRT Ehrlichia chaffeensis 14 Met Glu Asn Leu Met Asn Lys Lys Asn Lys Phe Phe Thr Ile Ser Thr 1 5 10 15 Ala Met Val Cys Leu Leu Leu Leu Pro Gly Ile Ser Phe Ser Glu Thr 20 25 30 Ile Asn Asn Ser Ala Lys Lys Gln Pro Gly Leu Tyr Ile Ser Gly Gln 35 40 45 Tyr Lys Pro Ser Val Ser Val Phe Ser Asn Phe Ser Val Lys Glu Thr 50 55 60 Asn Val Pro Thr Lys Gln Leu Ile Ala Leu Lys Lys Asp Ile Asn Ser 65 70 75 80 Val Ala Val Gly Ser Asn Ala Thr Thr Gly Ile Ser Asn Pro Gly Asn 85 90 95 Phe Thr Ile Pro Tyr Thr Ala Glu Phe Gln Asp Asn Val Ala Asn Phe 100 105 110 Asn Gly Ala Val Gly Tyr Ser Phe Pro Asp Ser Leu Arg Ile Glu Ile 115 120 125 Glu Gly Phe His Glu Lys Phe Asp Val Lys Asn Pro Gly Gly Tyr Thr 130 135 140 Gln Val Lys Asp Ala Tyr Arg Tyr Phe Ala Leu Ala Arg Asp Leu Lys 145 150 155 160 Asp Gly Phe Phe Glu Pro Lys Ala Glu Asp Thr Gly Val Tyr His Thr 165 170 175 Val Met Lys Asn Asp Gly Leu Ser Ile Leu Ser Thr Met Val Asn Val 180 185 190 Cys Tyr Asp Phe Ser Val Asp Glu Leu Pro Val Leu Pro Tyr Ile Cys 195 200 205 Ala Gly Met Gly Ile Asn Ala Ile Glu Phe Phe Asp Ala Leu His Val 210 215 220 Lys Phe Ala Tyr Gln Gly Lys Leu Gly Ile Ser Tyr Gln Leu Phe Thr 225 230 235 240 Lys Val Asn Leu Phe Leu Asp Gly Tyr Tyr His Gln Val Ile Gly Asn 245 250 255 Gln Phe Lys Asn Leu Asn Val Asn His Val Tyr Thr Leu Lys Glu Ser 260 265 270 Pro Lys Val Thr Ser Ala Val Ala Thr Leu Asp Ile Ala Tyr Phe Gly 275 280 285 Gly Glu Val Gly Ile Arg Phe Thr Phe 290 295 15 591 DNA Ehrlichia chaffeensis CDS (1)..(591) 15 atg ata tat aaa gaa aaa ctt act aga gtg gga gaa tat atc tta gca 48 Met Ile Tyr Lys Glu Lys Leu Thr Arg Val Gly Glu Tyr Ile Leu Ala 1 5 10 15 tat tta tca ttt att ctt tct act tat atc ttt cta gtg ctg gta aat 96 Tyr Leu Ser Phe Ile Leu Ser Thr Tyr Ile Phe Leu Val Leu Val Asn 20 25 30 att att aga tat aac agc ctt gct ata tgt gtt atc agt cta cta aga 144 Ile Ile Arg Tyr Asn Ser Leu Ala Ile Cys Val Ile Ser Leu Leu Arg 35 40 45 act aat atc ttt aac gtt agc aca aaa aaa tta ata aaa gat aaa tgt 192 Thr Asn Ile Phe Asn Val Ser Thr Lys Lys Leu Ile Lys Asp Lys Cys 50 55 60 cgt gat act aag ttt agt aac atg aat tgt tat ttg tac ggt aaa ccg 240 Arg Asp Thr Lys Phe Ser Asn Met Asn Cys Tyr Leu Tyr Gly Lys Pro 65 70 75 80 tta aat tta caa att ttt tat gga ata ttt tcc ttt att aga aac ttt 288 Leu Asn Leu Gln Ile Phe Tyr Gly Ile Phe Ser Phe Ile Arg Asn Phe 85 90 95 caa aat aac aca cta ata att cct aat gat agt aaa tgc ggc ttc tat 336 Gln Asn Asn Thr Leu Ile Ile Pro Asn Asp Ser Lys Cys Gly Phe Tyr 100 105 110 acc acg tta tgg gat aat cca gca cta cat tat aca tat aca ctt act 384 Thr Thr Leu Trp Asp Asn Pro Ala Leu His Tyr Thr Tyr Thr Leu Thr 115 120 125 ggc agt gag tac cgt aat ttt ttt gac att cta tat gaa aac att atc 432 Gly Ser Glu Tyr Arg Asn Phe Phe Asp Ile Leu Tyr Glu Asn Ile Ile 130 135 140 tgt caa tgt aaa tta ctt att aac tat aac cgt tct gta tta aac caa 480 Cys Gln Cys Lys Leu Leu Ile Asn Tyr Asn Arg Ser Val Leu Asn Gln 145 150 155 160 cat aat aaa aat act ctc gta ata ata cca ata cct aat gct aga gag 528 His Asn Lys Asn Thr Leu Val Ile Ile Pro Ile Pro Asn Ala Arg Glu 165 170 175 ttc agt aat gaa att cga gta agg aat ata tca ata aat aag gaa agt 576 Phe Ser Asn Glu Ile Arg Val Arg Asn Ile Ser Ile Asn Lys Glu Ser 180 185 190 tct tat gag tgc taa 591 Ser Tyr Glu Cys 195 16 196 PRT Ehrlichia chaffeensis 16 Met Ile Tyr Lys Glu Lys Leu Thr Arg Val Gly Glu Tyr Ile Leu Ala 1 5 10 15 Tyr Leu Ser Phe Ile Leu Ser Thr Tyr Ile Phe Leu Val Leu Val Asn 20 25 30 Ile Ile Arg Tyr Asn Ser Leu Ala Ile Cys Val Ile Ser Leu Leu Arg 35 40 45 Thr Asn Ile Phe Asn Val Ser Thr Lys Lys Leu Ile Lys Asp Lys Cys 50 55 60 Arg Asp Thr Lys Phe Ser Asn Met Asn Cys Tyr Leu Tyr Gly Lys Pro 65 70 75 80 Leu Asn Leu Gln Ile Phe Tyr Gly Ile Phe Ser Phe Ile Arg Asn Phe 85 90 95 Gln Asn Asn Thr Leu Ile Ile Pro Asn Asp Ser Lys Cys Gly Phe Tyr 100 105 110 Thr Thr Leu Trp Asp Asn Pro Ala Leu His Tyr Thr Tyr Thr Leu Thr 115 120 125 Gly Ser Glu Tyr Arg Asn Phe Phe Asp Ile Leu Tyr Glu Asn Ile Ile 130 135 140 Cys Gln Cys Lys Leu Leu Ile Asn Tyr Asn Arg Ser Val Leu Asn Gln 145 150 155 160 His Asn Lys Asn Thr Leu Val Ile Ile Pro Ile Pro Asn Ala Arg Glu 165 170 175 Phe Ser Asn Glu Ile Arg Val Arg Asn Ile Ser Ile Asn Lys Glu Ser 180 185 190 Ser Tyr Glu Cys 195 17 876 DNA Ehrlichia chaffeensis CDS (1)..(876) 17 atg aat aaa aaa aac aag ttt att ata gct aca gca ttg gta tat tta 48 Met Asn Lys Lys Asn Lys Phe Ile Ile Ala Thr Ala Leu Val Tyr Leu 1 5 10 15 ctg tca tta cct agt gta tcg ttt tca gag gtt aca aac agc agt att 96 Leu Ser Leu Pro Ser Val Ser Phe Ser Glu Val Thr Asn Ser Ser Ile 20 25 30 aaa aaa cac tct ggg tta tat att agt gga caa tac aaa cca agt gtt 144 Lys Lys His Ser Gly Leu Tyr Ile Ser Gly Gln Tyr Lys Pro Ser Val 35 40 45 tct gtt ttt agt agt ttc tca att aaa gaa act aac act atc aca aaa 192 Ser Val Phe Ser Ser Phe Ser Ile Lys Glu Thr Asn Thr Ile Thr Lys 50 55 60 aat ctt ata gcg tta aaa aaa gat att aac tct ctt gaa gtt aac gcc 240 Asn Leu Ile Ala Leu Lys Lys Asp Ile Asn Ser Leu Glu Val Asn Ala 65 70 75 80 gat gct agt caa ggt att agt cat cca gga aat ttt act ata cct tat 288 Asp Ala Ser Gln Gly Ile Ser His Pro Gly Asn Phe Thr Ile Pro Tyr 85 90 95 ata gca gca ttt gaa gat aat gct ttt aat ttc aac ggt gct att ggt 336 Ile Ala Ala Phe Glu Asp Asn Ala Phe Asn Phe Asn Gly Ala Ile Gly 100 105 110 tac att act gaa ggt cta agg att gaa ata gaa ggt tcc tat gaa gaa 384 Tyr Ile Thr Glu Gly Leu Arg Ile Glu Ile Glu Gly Ser Tyr Glu Glu 115 120 125 ttt gat gct aaa aac cct gga ggt tat ggt cta aat gat gcc ttt cgg 432 Phe Asp Ala Lys Asn Pro Gly Gly Tyr Gly Leu Asn Asp Ala Phe Arg 130 135 140 tac ttt gct tta gca cgt gat atg gaa agc aac aag ttc caa cca aaa 480 Tyr Phe Ala Leu Ala Arg Asp Met Glu Ser Asn Lys Phe Gln Pro Lys 145 150 155 160 gca caa agc tca caa aaa gta ttt cac act gta atg aag agt gat ggg 528 Ala Gln Ser Ser Gln Lys Val Phe His Thr Val Met Lys Ser Asp Gly 165 170 175 tta tct ata ata tct atc atg gtt aac ggc tgt tat gat ttt tct tcg 576 Leu Ser Ile Ile Ser Ile Met Val Asn Gly Cys Tyr Asp Phe Ser Ser 180 185 190 gat aat tta tta gta tca cct tat ata tgt gga ggt ata ggt gtg gat 624 Asp Asn Leu Leu Val Ser Pro Tyr Ile Cys Gly Gly Ile Gly Val Asp 195 200 205 gca ata gaa ttt ttt gac gca tta cac att aaa ctt gcg tgc caa agc 672 Ala Ile Glu Phe Phe Asp Ala Leu His Ile Lys Leu Ala Cys Gln Ser 210 215 220 aaa tta ggc atc act tat caa tta tct tat aat atc agc tta ttt gct 720 Lys Leu Gly Ile Thr Tyr Gln Leu Ser Tyr Asn Ile Ser Leu Phe Ala 225 230 235 240 gat gga tat tat cat caa gta ata ggt aac caa ttc aga aat tta aac 768 Asp Gly Tyr Tyr His Gln Val Ile Gly Asn Gln Phe Arg Asn Leu Asn 245 250 255 gtt caa cat gta gct gaa ctt aat gat gca cct aaa gtt aca tct gca 816 Val Gln His Val Ala Glu Leu Asn Asp Ala Pro Lys Val Thr Ser Ala 260 265 270 gtt gcc aca ctt aat gtt gga tat ttc ggc gct gaa gtt gga gta aga 864 Val Ala Thr Leu Asn Val Gly Tyr Phe Gly Ala Glu Val Gly Val Arg 275 280 285 ttt ata ttt taa 876 Phe Ile Phe 290 18 291 PRT Ehrlichia chaffeensis 18 Met Asn Lys Lys Asn Lys Phe Ile Ile Ala Thr Ala Leu Val Tyr Leu 1 5 10 15 Leu Ser Leu Pro Ser Val Ser Phe Ser Glu Val Thr Asn Ser Ser Ile 20 25 30 Lys Lys His Ser Gly Leu Tyr Ile Ser Gly Gln Tyr Lys Pro Ser Val 35 40 45 Ser Val Phe Ser Ser Phe Ser Ile Lys Glu Thr Asn Thr Ile Thr Lys 50 55 60 Asn Leu Ile Ala Leu Lys Lys Asp Ile Asn Ser Leu Glu Val Asn Ala 65 70 75 80 Asp Ala Ser Gln Gly Ile Ser His Pro Gly Asn Phe Thr Ile Pro Tyr 85 90 95 Ile Ala Ala Phe Glu Asp Asn Ala Phe Asn Phe Asn Gly Ala Ile Gly 100 105 110 Tyr Ile Thr Glu Gly Leu Arg Ile Glu Ile Glu Gly Ser Tyr Glu Glu 115 120 125 Phe Asp Ala Lys Asn Pro Gly Gly Tyr Gly Leu Asn Asp Ala Phe Arg 130 135 140 Tyr Phe Ala Leu Ala Arg Asp Met Glu Ser Asn Lys Phe Gln Pro Lys 145 150 155 160 Ala Gln Ser Ser Gln Lys Val Phe His Thr Val Met Lys Ser Asp Gly 165 170 175 Leu Ser Ile Ile Ser Ile Met Val Asn Gly Cys Tyr Asp Phe Ser Ser 180 185 190 Asp Asn Leu Leu Val Ser Pro Tyr Ile Cys Gly Gly Ile Gly Val Asp 195 200 205 Ala Ile Glu Phe Phe Asp Ala Leu His Ile Lys Leu Ala Cys Gln Ser 210 215 220 Lys Leu Gly Ile Thr Tyr Gln Leu Ser Tyr Asn Ile Ser Leu Phe Ala 225 230 235 240 Asp Gly Tyr Tyr His Gln Val Ile Gly Asn Gln Phe Arg Asn Leu Asn 245 250 255 Val Gln His Val Ala Glu Leu Asn Asp Ala Pro Lys Val Thr Ser Ala 260 265 270 Val Ala Thr Leu Asn Val Gly Tyr Phe Gly Ala Glu Val Gly Val Arg 275 280 285 Phe Ile Phe 290 19 396 DNA Ehrlichia chaffeensis CDS (1)..(396) 19 tct aga ata cat gat gaa aat tat gct att aca aca aat aat aaa tta 48 Ser Arg Ile His Asp Glu Asn Tyr Ala Ile Thr Thr Asn Asn Lys Leu 1 5 10 15 tcc atc gca tct att atg gtt aac acc tgc tat gat att tca att aat 96 Ser Ile Ala Ser Ile Met Val Asn Thr Cys Tyr Asp Ile Ser Ile Asn 20 25 30 aat aca tca ata gta ccg tat tta tgc aca ggc att ggt gaa gat ctt 144 Asn Thr Ser Ile Val Pro Tyr Leu Cys Thr Gly Ile Gly Glu Asp Leu 35 40 45 gta ggg ctt ttt aat aca ata cat ttt aaa ctt gca tat caa ggg aaa 192 Val Gly Leu Phe Asn Thr Ile His Phe Lys Leu Ala Tyr Gln Gly Lys 50 55 60 gtt gga atg agt tat ttg ata aat aac aat atc cta tta ttt tct gac 240 Val Gly Met Ser Tyr Leu Ile Asn Asn Asn Ile Leu Leu Phe Ser Asp 65 70 75 80 ata tat tat cat aaa gtc atg ggt aac aga ttt aaa aat ttg tac atg 288 Ile Tyr Tyr His Lys Val Met Gly Asn Arg Phe Lys Asn Leu Tyr Met 85 90 95 caa tat gta gct gat cct aat att tct gaa gaa act ata cct ata tta 336 Gln Tyr Val Ala Asp Pro Asn Ile Ser Glu Glu Thr Ile Pro Ile Leu 100 105 110 gca aaa ctt gat att ggt tat ttt gga agt gaa att gga ata agg ttt 384 Ala Lys Leu Asp Ile Gly Tyr Phe Gly Ser Glu Ile Gly Ile Arg Phe 115 120 125 atg ttt aac taa 396 Met Phe Asn 130 20 131 PRT Ehrlichia chaffeensis 20 Ser Arg Ile His Asp Glu Asn Tyr Ala Ile Thr Thr Asn Asn Lys Leu 1 5 10 15 Ser Ile Ala Ser Ile Met Val Asn Thr Cys Tyr Asp Ile Ser Ile Asn 20 25 30 Asn Thr Ser Ile Val Pro Tyr Leu Cys Thr Gly Ile Gly Glu Asp Leu 35 40 45 Val Gly Leu Phe Asn Thr Ile His Phe Lys Leu Ala Tyr Gln Gly Lys 50 55 60 Val Gly Met Ser Tyr Leu Ile Asn Asn Asn Ile Leu Leu Phe Ser Asp 65 70 75 80 Ile Tyr Tyr His Lys Val Met Gly Asn Arg Phe Lys Asn Leu Tyr Met 85 90 95 Gln Tyr Val Ala Asp Pro Asn Ile Ser Glu Glu Thr Ile Pro Ile Leu 100 105 110 Ala Lys Leu Asp Ile Gly Tyr Phe Gly Ser Glu Ile Gly Ile Arg Phe 115 120 125 Met Phe Asn 130 21 888 DNA Ehrlichia chaffeensis CDS (1)..(888) 21 atg aca aag aaa ttt aat ttt gta aat gtt ata tta aca ttt ttg tta 48 Met Thr Lys Lys Phe Asn Phe Val Asn Val Ile Leu Thr Phe Leu Leu 1 5 10 15 ttt ctt ttc cca ctt aag tca ttt aca aca tat gca aat aat aac aca 96 Phe Leu Phe Pro Leu Lys Ser Phe Thr Thr Tyr Ala Asn Asn Asn Thr 20 25 30 atc act caa aaa gtt gga ttg tac ata agt ggt caa tat aag cca agt 144 Ile Thr Gln Lys Val Gly Leu Tyr Ile Ser Gly Gln Tyr Lys Pro Ser 35 40 45 att cct cat ttc aag aat ttt tca gta gaa gaa aat gac aaa gta gta 192 Ile Pro His Phe Lys Asn Phe Ser Val Glu Glu Asn Asp Lys Val Val 50 55 60 gat ttg ata ggt ctt aca act gat gtt aca tat atc aca gaa cat ata 240 Asp Leu Ile Gly Leu Thr Thr Asp Val Thr Tyr Ile Thr Glu His Ile 65 70 75 80 tta cga gat aat aca aaa ttc aac act cat tat att gca aag ttc aag 288 Leu Arg Asp Asn Thr Lys Phe Asn Thr His Tyr Ile Ala Lys Phe Lys 85 90 95 aac aat ttt ata aat ttc agc agt gca att ggt tat tat tct ggg caa 336 Asn Asn Phe Ile Asn Phe Ser Ser Ala Ile Gly Tyr Tyr Ser Gly Gln 100 105 110 gga cca agg tta gaa ata gaa agc tct tat ggg gat ttt gat gtt gta 384 Gly Pro Arg Leu Glu Ile Glu Ser Ser Tyr Gly Asp Phe Asp Val Val 115 120 125 aat tat aaa aat tat gca gta caa gat gtt aat aga tat ttt gct tta 432 Asn Tyr Lys Asn Tyr Ala Val Gln Asp Val Asn Arg Tyr Phe Ala Leu 130 135 140 gta cgt gaa aaa aat ggt tca aat ttc tct cca aaa cca cat gaa act 480 Val Arg Glu Lys Asn Gly Ser Asn Phe Ser Pro Lys Pro His Glu Thr 145 150 155 160 agt caa ccc tct gac agt aat cct aaa aag tct ttt tat act tta atg 528 Ser Gln Pro Ser Asp Ser Asn Pro Lys Lys Ser Phe Tyr Thr Leu Met 165 170 175 aag aat aat ggg gta ttt gtt gca tca gta ata atc aac ggt tgt tat 576 Lys Asn Asn Gly Val Phe Val Ala Ser Val Ile Ile Asn Gly Cys Tyr 180 185 190 gat ttt tct ttt aat aac aca aca ata tca cct tac gta tgt ata gga 624 Asp Phe Ser Phe Asn Asn Thr Thr Ile Ser Pro Tyr Val Cys Ile Gly 195 200 205 gtt gga gga gat ttt ata gag ttt ttt gaa gta atg cat atc aag ttt 672 Val Gly Gly Asp Phe Ile Glu Phe Phe Glu Val Met His Ile Lys Phe 210 215 220 gct tgc caa agt aag gtt ggt att agc tat cca ata tct ccc tct att 720 Ala Cys Gln Ser Lys Val Gly Ile Ser Tyr Pro Ile Ser Pro Ser Ile 225 230 235 240 act att ttt gct gat gca vat tat cac aag gtc ata aat aat aaa ttt 768 Thr Ile Phe Ala Asp Ala Xaa Tyr His Lys Val Ile Asn Asn Lys Phe 245 250 255 aac aac cta cat gtt aag tat tca tat gaa ctt aaa aac tca cct acc 816 Asn Asn Leu His Val Lys Tyr Ser Tyr Glu Leu Lys Asn Ser Pro Thr 260 265 270 att acc tct gca aca gcc aaa cta aac att gaa tat ttt ggt ggt gaa 864 Ile Thr Ser Ala Thr Ala Lys Leu Asn Ile Glu Tyr Phe Gly Gly Glu 275 280 285 gtt ggg atg aga ttt ata ttt taa 888 Val Gly Met Arg Phe Ile Phe 290 295 22 295 PRT Ehrlichia chaffeensis 22 Met Thr Lys Lys Phe Asn Phe Val Asn Val Ile Leu Thr Phe Leu Leu 1 5 10 15 Phe Leu Phe Pro Leu Lys Ser Phe Thr Thr Tyr Ala Asn Asn Asn Thr 20 25 30 Ile Thr Gln Lys Val Gly Leu Tyr Ile Ser Gly Gln Tyr Lys Pro Ser 35 40 45 Ile Pro His Phe Lys Asn Phe Ser Val Glu Glu Asn Asp Lys Val Val 50 55 60 Asp Leu Ile Gly Leu Thr Thr Asp Val Thr Tyr Ile Thr Glu His Ile 65 70 75 80 Leu Arg Asp Asn Thr Lys Phe Asn Thr His Tyr Ile Ala Lys Phe Lys 85 90 95 Asn Asn Phe Ile Asn Phe Ser Ser Ala Ile Gly Tyr Tyr Ser Gly Gln 100 105 110 Gly Pro Arg Leu Glu Ile Glu Ser Ser Tyr Gly Asp Phe Asp Val Val 115 120 125 Asn Tyr Lys Asn Tyr Ala Val Gln Asp Val Asn Arg Tyr Phe Ala Leu 130 135 140 Val Arg Glu Lys Asn Gly Ser Asn Phe Ser Pro Lys Pro His Glu Thr 145 150 155 160 Ser Gln Pro Ser Asp Ser Asn Pro Lys Lys Ser Phe Tyr Thr Leu Met 165 170 175 Lys Asn Asn Gly Val Phe Val Ala Ser Val Ile Ile Asn Gly Cys Tyr 180 185 190 Asp Phe Ser Phe Asn Asn Thr Thr Ile Ser Pro Tyr Val Cys Ile Gly 195 200 205 Val Gly Gly Asp Phe Ile Glu Phe Phe Glu Val Met His Ile Lys Phe 210 215 220 Ala Cys Gln Ser Lys Val Gly Ile Ser Tyr Pro Ile Ser Pro Ser Ile 225 230 235 240 Thr Ile Phe Ala Asp Ala Xaa Tyr His Lys Val Ile Asn Asn Lys Phe 245 250 255 Asn Asn Leu His Val Lys Tyr Ser Tyr Glu Leu Lys Asn Ser Pro Thr 260 265 270 Ile Thr Ser Ala Thr Ala Lys Leu Asn Ile Glu Tyr Phe Gly Gly Glu 275 280 285 Val Gly Met Arg Phe Ile Phe 290 295 23 840 DNA Ehrlichia chaffeensis CDS (1)..(840) 23 atg agc aaa aaa aag ttt att aca ata gga aca gta ctt gca tct cta 48 Met Ser Lys Lys Lys Phe Ile Thr Ile Gly Thr Val Leu Ala Ser Leu 1 5 10 15 tta tca ttc tta tct att gaa tcc ttt tca gct ata aat cat aat cat 96 Leu Ser Phe Leu Ser Ile Glu Ser Phe Ser Ala Ile Asn His Asn His 20 25 30 aca gga aat aac act agt ggt ata tat att aca ggg cag tat aga cca 144 Thr Gly Asn Asn Thr Ser Gly Ile Tyr Ile Thr Gly Gln Tyr Arg Pro 35 40 45 gga gta tcc cat ttt agc aat ttc tca gta aaa gaa act aat gtt gat 192 Gly Val Ser His Phe Ser Asn Phe Ser Val Lys Glu Thr Asn Val Asp 50 55 60 aca ata caa cta gta gga tat aaa aaa agt gcg tct tct atc gat cct 240 Thr Ile Gln Leu Val Gly Tyr Lys Lys Ser Ala Ser Ser Ile Asp Pro 65 70 75 80 aac act tat tca aac ttt caa ggt cca tat act gtt aca ttt caa gat 288 Asn Thr Tyr Ser Asn Phe Gln Gly Pro Tyr Thr Val Thr Phe Gln Asp 85 90 95 aat gct gct agt ttc agt gga gca att gga tat tct tac ccc gaa agt 336 Asn Ala Ala Ser Phe Ser Gly Ala Ile Gly Tyr Ser Tyr Pro Glu Ser 100 105 110 cta aga ctt gaa ctt gaa ggt tct tac gaa aaa ttt gat gtc aaa gat 384 Leu Arg Leu Glu Leu Glu Gly Ser Tyr Glu Lys Phe Asp Val Lys Asp 115 120 125 cct aaa gac tac tca gca aaa gat gct ttt agg ttt ttt gct cta gca 432 Pro Lys Asp Tyr Ser Ala Lys Asp Ala Phe Arg Phe Phe Ala Leu Ala 130 135 140 cgt aat acg tct act act gtt cct gat gct caa aaa tat aca gtt atg 480 Arg Asn Thr Ser Thr Thr Val Pro Asp Ala Gln Lys Tyr Thr Val Met 145 150 155 160 aag aat aat ggc tta tct gtt gca tca atc atg atc aat ggt tgt tat 528 Lys Asn Asn Gly Leu Ser Val Ala Ser Ile Met Ile Asn Gly Cys Tyr 165 170 175 gat cta tct ttt aat aat tta gtc gta tca cct tat ata tgt gca ggt 576 Asp Leu Ser Phe Asn Asn Leu Val Val Ser Pro Tyr Ile Cys Ala Gly 180 185 190 att ggt gaa gat ttc att gaa ttt ttt gat act ttg cac att aaa ctt 624 Ile Gly Glu Asp Phe Ile Glu Phe Phe Asp Thr Leu His Ile Lys Leu 195 200 205 gct tat caa gga aaa cta ggt att agt tat tac ttc ttt cct aag att 672 Ala Tyr Gln Gly Lys Leu Gly Ile Ser Tyr Tyr Phe Phe Pro Lys Ile 210 215 220 aat gta ttt gct ggt ggg tac tat cat aga gtt ata ggg aat aaa ttt 720 Asn Val Phe Ala Gly Gly Tyr Tyr His Arg Val Ile Gly Asn Lys Phe 225 230 235 240 aaa aat tta aat gtt aac cat gtt gtt aca ctt gat gaa ttt cct aaa 768 Lys Asn Leu Asn Val Asn His Val Val Thr Leu Asp Glu Phe Pro Lys 245 250 255 gca act tct gca gta gct aca ctt aat gtt gct tat ttt ggt ggt gaa 816 Ala Thr Ser Ala Val Ala Thr Leu Asn Val Ala Tyr Phe Gly Gly Glu 260 265 270 gct gga gta aag ttt aca ttt taa 840 Ala Gly Val Lys Phe Thr Phe 275 280 24 279 PRT Ehrlichia chaffeensis 24 Met Ser Lys Lys Lys Phe Ile Thr Ile Gly Thr Val Leu Ala Ser Leu 1 5 10 15 Leu Ser Phe Leu Ser Ile Glu Ser Phe Ser Ala Ile Asn His Asn His 20 25 30 Thr Gly Asn Asn Thr Ser Gly Ile Tyr Ile Thr Gly Gln Tyr Arg Pro 35 40 45 Gly Val Ser His Phe Ser Asn Phe Ser Val Lys Glu Thr Asn Val Asp 50 55 60 Thr Ile Gln Leu Val Gly Tyr Lys Lys Ser Ala Ser Ser Ile Asp Pro 65 70 75 80 Asn Thr Tyr Ser Asn Phe Gln Gly Pro Tyr Thr Val Thr Phe Gln Asp 85 90 95 Asn Ala Ala Ser Phe Ser Gly Ala Ile Gly Tyr Ser Tyr Pro Glu Ser 100 105 110 Leu Arg Leu Glu Leu Glu Gly Ser Tyr Glu Lys Phe Asp Val Lys Asp 115 120 125 Pro Lys Asp Tyr Ser Ala Lys Asp Ala Phe Arg Phe Phe Ala Leu Ala 130 135 140 Arg Asn Thr Ser Thr Thr Val Pro Asp Ala Gln Lys Tyr Thr Val Met 145 150 155 160 Lys Asn Asn Gly Leu Ser Val Ala Ser Ile Met Ile Asn Gly Cys Tyr 165 170 175 Asp Leu Ser Phe Asn Asn Leu Val Val Ser Pro Tyr Ile Cys Ala Gly 180 185 190 Ile Gly Glu Asp Phe Ile Glu Phe Phe Asp Thr Leu His Ile Lys Leu 195 200 205 Ala Tyr Gln Gly Lys Leu Gly Ile Ser Tyr Tyr Phe Phe Pro Lys Ile 210 215 220 Asn Val Phe Ala Gly Gly Tyr Tyr His Arg Val Ile Gly Asn Lys Phe 225 230 235 240 Lys Asn Leu Asn Val Asn His Val Val Thr Leu Asp Glu Phe Pro Lys 245 250 255 Ala Thr Ser Ala Val Ala Thr Leu Asn Val Ala Tyr Phe Gly Gly Glu 260 265 270 Ala Gly Val Lys Phe Thr Phe 275 25 852 DNA Ehrlichia chaffeensis CDS (1)..(852) 25 atg agt gct aaa aaa aag ctt ttt ata ata ggg tca gtg tta gta tgt 48 Met Ser Ala Lys Lys Lys Leu Phe Ile Ile Gly Ser Val Leu Val Cys 1 5 10 15 tta gtg tca tac tta cct act aaa tct ttg tca aac tta aat aat att 96 Leu Val Ser Tyr Leu Pro Thr Lys Ser Leu Ser Asn Leu Asn Asn Ile 20 25 30 aat aat aac act aag tgc act ggg cta tat gtc agt gga caa tat aaa 144 Asn Asn Asn Thr Lys Cys Thr Gly Leu Tyr Val Ser Gly Gln Tyr Lys 35 40 45 cct act gtt tct cac ttt agt aat ttt tca ctt aaa gaa act tat act 192 Pro Thr Val Ser His Phe Ser Asn Phe Ser Leu Lys Glu Thr Tyr Thr 50 55 60 gac act aaa gag tta tta gga cta gca aaa gat att aag tct att aca 240 Asp Thr Lys Glu Leu Leu Gly Leu Ala Lys Asp Ile Lys Ser Ile Thr 65 70 75 80 gat ata aca aca aat aaa aaa ttc aac att cct tat aac aca aaa ttt 288 Asp Ile Thr Thr Asn Lys Lys Phe Asn Ile Pro Tyr Asn Thr Lys Phe 85 90 95 caa gat aat gct gtt agc ttc agt gca gct gtt gga tat att tcc caa 336 Gln Asp Asn Ala Val Ser Phe Ser Ala Ala Val Gly Tyr Ile Ser Gln 100 105 110 gac agt cca agg gtt gag gta gaa tgg tct tat gaa gaa ttt gac gtt 384 Asp Ser Pro Arg Val Glu Val Glu Trp Ser Tyr Glu Glu Phe Asp Val 115 120 125 aaa aat cct ggt aat tac gta gta agt gaa gcc ttc agg tat att gct 432 Lys Asn Pro Gly Asn Tyr Val Val Ser Glu Ala Phe Arg Tyr Ile Ala 130 135 140 tta gca aga gga att gat aat ctt caa aaa tat cct gaa aca aat aag 480 Leu Ala Arg Gly Ile Asp Asn Leu Gln Lys Tyr Pro Glu Thr Asn Lys 145 150 155 160 tat gtt gtt ata aag aac aat ggc tta tct gtc gca tcc att ata atc 528 Tyr Val Val Ile Lys Asn Asn Gly Leu Ser Val Ala Ser Ile Ile Ile 165 170 175 aat ggc tgt tat gat ttt tct tta aac aat tta aaa gta tca cct tac 576 Asn Gly Cys Tyr Asp Phe Ser Leu Asn Asn Leu Lys Val Ser Pro Tyr 180 185 190 ata tgc gta ggg ttt ggt ggg gac att ata gaa ttt ttt agt gct gta 624 Ile Cys Val Gly Phe Gly Gly Asp Ile Ile Glu Phe Phe Ser Ala Val 195 200 205 agt ttt aaa ttt gct tat caa ggt aag gta ggt atc agt tat cca tta 672 Ser Phe Lys Phe Ala Tyr Gln Gly Lys Val Gly Ile Ser Tyr Pro Leu 210 215 220 ttc tct aat atg att ata ttt gct gac gga tat tac cat aag gtc ata 720 Phe Ser Asn Met Ile Ile Phe Ala Asp Gly Tyr Tyr His Lys Val Ile 225 230 235 240 gga aat aaa ttt aac aat tta aat gtt caa cac gtt gtt agt ctt aac 768 Gly Asn Lys Phe Asn Asn Leu Asn Val Gln His Val Val Ser Leu Asn 245 250 255 agt cat cct aag tct act ttt gca gta gct act ctt aat gtt gag tat 816 Ser His Pro Lys Ser Thr Phe Ala Val Ala Thr Leu Asn Val Glu Tyr 260 265 270 ttc ggt agt gaa ttt ggg tta aaa ttt ata ttt taa 852 Phe Gly Ser Glu Phe Gly Leu Lys Phe Ile Phe 275 280 26 283 PRT Ehrlichia chaffeensis 26 Met Ser Ala Lys Lys Lys Leu Phe Ile Ile Gly Ser Val Leu Val Cys 1 5 10 15 Leu Val Ser Tyr Leu Pro Thr Lys Ser Leu Ser Asn Leu Asn Asn Ile 20 25 30 Asn Asn Asn Thr Lys Cys Thr Gly Leu Tyr Val Ser Gly Gln Tyr Lys 35 40 45 Pro Thr Val Ser His Phe Ser Asn Phe Ser Leu Lys Glu Thr Tyr Thr 50 55 60 Asp Thr Lys Glu Leu Leu Gly Leu Ala Lys Asp Ile Lys Ser Ile Thr 65 70 75 80 Asp Ile Thr Thr Asn Lys Lys Phe Asn Ile Pro Tyr Asn Thr Lys Phe 85 90 95 Gln Asp Asn Ala Val Ser Phe Ser Ala Ala Val Gly Tyr Ile Ser Gln 100 105 110 Asp Ser Pro Arg Val Glu Val Glu Trp Ser Tyr Glu Glu Phe Asp Val 115 120 125 Lys Asn Pro Gly Asn Tyr Val Val Ser Glu Ala Phe Arg Tyr Ile Ala 130 135 140 Leu Ala Arg Gly Ile Asp Asn Leu Gln Lys Tyr Pro Glu Thr Asn Lys 145 150 155 160 Tyr Val Val Ile Lys Asn Asn Gly Leu Ser Val Ala Ser Ile Ile Ile 165 170 175 Asn Gly Cys Tyr Asp Phe Ser Leu Asn Asn Leu Lys Val Ser Pro Tyr 180 185 190 Ile Cys Val Gly Phe Gly Gly Asp Ile Ile Glu Phe Phe Ser Ala Val 195 200 205 Ser Phe Lys Phe Ala Tyr Gln Gly Lys Val Gly Ile Ser Tyr Pro Leu 210 215 220 Phe Ser Asn Met Ile Ile Phe Ala Asp Gly Tyr Tyr His Lys Val Ile 225 230 235 240 Gly Asn Lys Phe Asn Asn Leu Asn Val Gln His Val Val Ser Leu Asn 245 250 255 Ser His Pro Lys Ser Thr Phe Ala Val Ala Thr Leu Asn Val Glu Tyr 260 265 270 Phe Gly Ser Glu Phe Gly Leu Lys Phe Ile Phe 275 280 27 828 DNA Ehrlichia chaffeensis CDS (1)..(828) 27 atg agt aaa aaa aat ttt att aca ata gga gca aca ctt att cat atg 48 Met Ser Lys Lys Asn Phe Ile Thr Ile Gly Ala Thr Leu Ile His Met 1 5 10 15 ttg tta cct aac ata tct ttt cca gaa act att aac aat aac act gat 96 Leu Leu Pro Asn Ile Ser Phe Pro Glu Thr Ile Asn Asn Asn Thr Asp 20 25 30 aaa ctt tct ggg tta tat ata agt ggg caa tat aaa cca ggg att tct 144 Lys Leu Ser Gly Leu Tyr Ile Ser Gly Gln Tyr Lys Pro Gly Ile Ser 35 40 45 cat ttc agc aaa ttt tca gtc aaa gaa atc tat aat gat aac att caa 192 His Phe Ser Lys Phe Ser Val Lys Glu Ile Tyr Asn Asp Asn Ile Gln 50 55 60 cta att ggg tta aga cac aac gca att tct act agt acc ctt aat att 240 Leu Ile Gly Leu Arg His Asn Ala Ile Ser Thr Ser Thr Leu Asn Ile 65 70 75 80 aat aca gat ttt aat atc ccc tat aaa gta aca ttt caa aat aac att 288 Asn Thr Asp Phe Asn Ile Pro Tyr Lys Val Thr Phe Gln Asn Asn Ile 85 90 95 acc agc ttt agt gga gct att ggt tat tct gat ccc aca ggg gca aga 336 Thr Ser Phe Ser Gly Ala Ile Gly Tyr Ser Asp Pro Thr Gly Ala Arg 100 105 110 ttt gag ctt gaa ggt tct tat gaa gaa ttt gat gtg aca gat cct gga 384 Phe Glu Leu Glu Gly Ser Tyr Glu Glu Phe Asp Val Thr Asp Pro Gly 115 120 125 gac tgc tta ata aaa gat acc tat aga tat ttc gct tta gct aga aac 432 Asp Cys Leu Ile Lys Asp Thr Tyr Arg Tyr Phe Ala Leu Ala Arg Asn 130 135 140 cca tca ggt tct agc cct acc tca aac aac tat act gtt atg aga aat 480 Pro Ser Gly Ser Ser Pro Thr Ser Asn Asn Tyr Thr Val Met Arg Asn 145 150 155 160 gat ggt gtt tcc att act tct gtt ata ttt aat ggc tgt tat gac atc 528 Asp Gly Val Ser Ile Thr Ser Val Ile Phe Asn Gly Cys Tyr Asp Ile 165 170 175 ttt tta aag gat tta gaa gta tca cct tat gta tgt gtt ggt gta ggt 576 Phe Leu Lys Asp Leu Glu Val Ser Pro Tyr Val Cys Val Gly Val Gly 180 185 190 gga gat ttt ata gaa ttt ttt gac gca tta cac att aaa tta gca tac 624 Gly Asp Phe Ile Glu Phe Phe Asp Ala Leu His Ile Lys Leu Ala Tyr 195 200 205 caa ggc aag tta ggt atc aat tat cac tta tcg act caa gca agc gta 672 Gln Gly Lys Leu Gly Ile Asn Tyr His Leu Ser Thr Gln Ala Ser Val 210 215 220 ttt att gat gga tat tat cat aag gtt ata gga aat caa ttc aac aat 720 Phe Ile Asp Gly Tyr Tyr His Lys Val Ile Gly Asn Gln Phe Asn Asn 225 230 235 240 cta aat gtt caa cac gtg gct agt aca gat ttt gga cct gta tac gca 768 Leu Asn Val Gln His Val Ala Ser Thr Asp Phe Gly Pro Val Tyr Ala 245 250 255 gta gcc aca ctt aac att ggt tat ttt ggt ggt gaa atc gga att aga 816 Val Ala Thr Leu Asn Ile Gly Tyr Phe Gly Gly Glu Ile Gly Ile Arg 260 265 270 ctt aca ttt taa 828 Leu Thr Phe 275 28 275 PRT Ehrlichia chaffeensis 28 Met Ser Lys Lys Asn Phe Ile Thr Ile Gly Ala Thr Leu Ile His Met 1 5 10 15 Leu Leu Pro Asn Ile Ser Phe Pro Glu Thr Ile Asn Asn Asn Thr Asp 20 25 30 Lys Leu Ser Gly Leu Tyr Ile Ser Gly Gln Tyr Lys Pro Gly Ile Ser 35 40 45 His Phe Ser Lys Phe Ser Val Lys Glu Ile Tyr Asn Asp Asn Ile Gln 50 55 60 Leu Ile Gly Leu Arg His Asn Ala Ile Ser Thr Ser Thr Leu Asn Ile 65 70 75 80 Asn Thr Asp Phe Asn Ile Pro Tyr Lys Val Thr Phe Gln Asn Asn Ile 85 90 95 Thr Ser Phe Ser Gly Ala Ile Gly Tyr Ser Asp Pro Thr Gly Ala Arg 100 105 110 Phe Glu Leu Glu Gly Ser Tyr Glu Glu Phe Asp Val Thr Asp Pro Gly 115 120 125 Asp Cys Leu Ile Lys Asp Thr Tyr Arg Tyr Phe Ala Leu Ala Arg Asn 130 135 140 Pro Ser Gly Ser Ser Pro Thr Ser Asn Asn Tyr Thr Val Met Arg Asn 145 150 155 160 Asp Gly Val Ser Ile Thr Ser Val Ile Phe Asn Gly Cys Tyr Asp Ile 165 170 175 Phe Leu Lys Asp Leu Glu Val Ser Pro Tyr Val Cys Val Gly Val Gly 180 185 190 Gly Asp Phe Ile Glu Phe Phe Asp Ala Leu His Ile Lys Leu Ala Tyr 195 200 205 Gln Gly Lys Leu Gly Ile Asn Tyr His Leu Ser Thr Gln Ala Ser Val 210 215 220 Phe Ile Asp Gly Tyr Tyr His Lys Val Ile Gly Asn Gln Phe Asn Asn 225 230 235 240 Leu Asn Val Gln His Val Ala Ser Thr Asp Phe Gly Pro Val Tyr Ala 245 250 255 Val Ala Thr Leu Asn Ile Gly Tyr Phe Gly Gly Glu Ile Gly Ile Arg 260 265 270 Leu Thr Phe 275 29 858 DNA Ehrlichia chaffeensis CDS (1)..(858) 29 atg aat aat aga aaa agt ttt ttt ata ata ggt gca tca tta cta gca 48 Met Asn Asn Arg Lys Ser Phe Phe Ile Ile Gly Ala Ser Leu Leu Ala 1 5 10 15 agc tta tta ttc aca tct gag gcc tct tct aca gga aat gta agt aac 96 Ser Leu Leu Phe Thr Ser Glu Ala Ser Ser Thr Gly Asn Val Ser Asn 20 25 30 cat act tat ttt aaa cct agg tta tat atc agt gga caa tat aga cca 144 His Thr Tyr Phe Lys Pro Arg Leu Tyr Ile Ser Gly Gln Tyr Arg Pro 35 40 45 gga gtt tct cat ttt agc aaa ttt tca gtc aaa gaa acc aac tac aat 192 Gly Val Ser His Phe Ser Lys Phe Ser Val Lys Glu Thr Asn Tyr Asn 50 55 60 act act caa cta gtt ggg ctt aaa aag gac atc agt gtc ata ggg aac 240 Thr Thr Gln Leu Val Gly Leu Lys Lys Asp Ile Ser Val Ile Gly Asn 65 70 75 80 agt aat atc aca acc tac aca aat ttc aac ttt cct tac att gca gaa 288 Ser Asn Ile Thr Thr Tyr Thr Asn Phe Asn Phe Pro Tyr Ile Ala Glu 85 90 95 ttt caa gac aat gcc ata agt ttc agt ggg gca att gga tac ttg tat 336 Phe Gln Asp Asn Ala Ile Ser Phe Ser Gly Ala Ile Gly Tyr Leu Tyr 100 105 110 tcc gag aat ttt aga att gaa gta gag gct tct tat gaa gaa ttt gat 384 Ser Glu Asn Phe Arg Ile Glu Val Glu Ala Ser Tyr Glu Glu Phe Asp 115 120 125 gtt aaa aat cca gaa gga tct gct aca gac gca tac agg tat ttt gca 432 Val Lys Asn Pro Glu Gly Ser Ala Thr Asp Ala Tyr Arg Tyr Phe Ala 130 135 140 cta gca cgt gct atg gat ggc act aat aaa tct agt cct gat gac aca 480 Leu Ala Arg Ala Met Asp Gly Thr Asn Lys Ser Ser Pro Asp Asp Thr 145 150 155 160 aga aaa ttc act gtc atg aga aat gac ggg tta tca att tca tca gta 528 Arg Lys Phe Thr Val Met Arg Asn Asp Gly Leu Ser Ile Ser Ser Val 165 170 175 atg ata aat ggg tgt tac aat ttt aca tta gat gat ata cca gta gta 576 Met Ile Asn Gly Cys Tyr Asn Phe Thr Leu Asp Asp Ile Pro Val Val 180 185 190 ccg tat gta tgc gca gga ata gga gga gat ttc ata gag ttt ttt aat 624 Pro Tyr Val Cys Ala Gly Ile Gly Gly Asp Phe Ile Glu Phe Phe Asn 195 200 205 gat tta cat gtt aag ttt cgt cat caa ggc aag gta ggt att agt tat 672 Asp Leu His Val Lys Phe Arg His Gln Gly Lys Val Gly Ile Ser Tyr 210 215 220 tct ata tcc cct gaa gta agt tta ttt ctt aac gga tat tac cat aaa 720 Ser Ile Ser Pro Glu Val Ser Leu Phe Leu Asn Gly Tyr Tyr His Lys 225 230 235 240 gta aca ggt aac aga ttt aaa aac tta cac gtt caa cac gta agt gat 768 Val Thr Gly Asn Arg Phe Lys Asn Leu His Val Gln His Val Ser Asp 245 250 255 tta agt gac gct cct aag ttc aca tct gca gtt gct aca ctc aat gtt 816 Leu Ser Asp Ala Pro Lys Phe Thr Ser Ala Val Ala Thr Leu Asn Val 260 265 270 ggg tac ttt ggt ggc gaa att gga gta aga ttt ata ttt taa 858 Gly Tyr Phe Gly Gly Glu Ile Gly Val Arg Phe Ile Phe 275 280 285 30 285 PRT Ehrlichia chaffeensis 30 Met Asn Asn Arg Lys Ser Phe Phe Ile Ile Gly Ala Ser Leu Leu Ala 1 5 10 15 Ser Leu Leu Phe Thr Ser Glu Ala Ser Ser Thr Gly Asn Val Ser Asn 20 25 30 His Thr Tyr Phe Lys Pro Arg Leu Tyr Ile Ser Gly Gln Tyr Arg Pro 35 40 45 Gly Val Ser His Phe Ser Lys Phe Ser Val Lys Glu Thr Asn Tyr Asn 50 55 60 Thr Thr Gln Leu Val Gly Leu Lys Lys Asp Ile Ser Val Ile Gly Asn 65 70 75 80 Ser Asn Ile Thr Thr Tyr Thr Asn Phe Asn Phe Pro Tyr Ile Ala Glu 85 90 95 Phe Gln Asp Asn Ala Ile Ser Phe Ser Gly Ala Ile Gly Tyr Leu Tyr 100 105 110 Ser Glu Asn Phe Arg Ile Glu Val Glu Ala Ser Tyr Glu Glu Phe Asp 115 120 125 Val Lys Asn Pro Glu Gly Ser Ala Thr Asp Ala Tyr Arg Tyr Phe Ala 130 135 140 Leu Ala Arg Ala Met Asp Gly Thr Asn Lys Ser Ser Pro Asp Asp Thr 145 150 155 160 Arg Lys Phe Thr Val Met Arg Asn Asp Gly Leu Ser Ile Ser Ser Val 165 170 175 Met Ile Asn Gly Cys Tyr Asn Phe Thr Leu Asp Asp Ile Pro Val Val 180 185 190 Pro Tyr Val Cys Ala Gly Ile Gly Gly Asp Phe Ile Glu Phe Phe Asn 195 200 205 Asp Leu His Val Lys Phe Arg His Gln Gly Lys Val Gly Ile Ser Tyr 210 215 220 Ser Ile Ser Pro Glu Val Ser Leu Phe Leu Asn Gly Tyr Tyr His Lys 225 230 235 240 Val Thr Gly Asn Arg Phe Lys Asn Leu His Val Gln His Val Ser Asp 245 250 255 Leu Ser Asp Ala Pro Lys Phe Thr Ser Ala Val Ala Thr Leu Asn Val 260 265 270 Gly Tyr Phe Gly Gly Glu Ile Gly Val Arg Phe Ile Phe 275 280 285 31 867 DNA Ehrlichia canis CDS (1)..(867) 31 atg aat tgc aaa aga ttt ttc ata gca agt gca ttg ata tca cta atg 48 Met Asn Cys Lys Arg Phe Phe Ile Ala Ser Ala Leu Ile Ser Leu Met 1 5 10 15 tct ttc tta cct agc gta tct ttt tct gaa tca ata cat gaa gat aat 96 Ser Phe Leu Pro Ser Val Ser Phe Ser Glu Ser Ile His Glu Asp Asn 20 25 30 ata aat ggt aac ttt tac att agt gca aag tat atg cca agt gcc tca 144 Ile Asn Gly Asn Phe Tyr Ile Ser Ala Lys Tyr Met Pro Ser Ala Ser 35 40 45 cac ttt ggc gta ttt tca gtt aaa gaa gag aaa aac aca aca act gga 192 His Phe Gly Val Phe Ser Val Lys Glu Glu Lys Asn Thr Thr Thr Gly 50 55 60 gtt ttc gga tta aaa caa gat tgg gac gga gca aca ata aag gat gca 240 Val Phe Gly Leu Lys Gln Asp Trp Asp Gly Ala Thr Ile Lys Asp Ala 65 70 75 80 agc agc agc cac aca ata gac cca agt aca ata ttc tcc att tca aat 288 Ser Ser Ser His Thr Ile Asp Pro Ser Thr Ile Phe Ser Ile Ser Asn 85 90 95 tat tca ttt aaa tat gaa aac aat cca ttt tta ggg ttt gca gga gct 336 Tyr Ser Phe Lys Tyr Glu Asn Asn Pro Phe Leu Gly Phe Ala Gly Ala 100 105 110 att ggc tac tca atg ggt ggt cca agg gta gag ttt gaa gtg tct tac 384 Ile Gly Tyr Ser Met Gly Gly Pro Arg Val Glu Phe Glu Val Ser Tyr 115 120 125 gaa ata ttt gat gta aaa aac caa ggt aac agt tac aag aac gat gct 432 Glu Ile Phe Asp Val Lys Asn Gln Gly Asn Ser Tyr Lys Asn Asp Ala 130 135 140 cac aaa tat tgc gct tta tca aga cac acc gga ggt atg cca caa gcc 480 His Lys Tyr Cys Ala Leu Ser Arg His Thr Gly Gly Met Pro Gln Ala 145 150 155 160 ggt cat caa aat aaa ttt gtc ttc cta aaa aat gaa gga tta ctt gac 528 Gly His Gln Asn Lys Phe Val Phe Leu Lys Asn Glu Gly Leu Leu Asp 165 170 175 ata tca ctt atg ata aac gca tgt tat gat ata aca atc gac agc atg 576 Ile Ser Leu Met Ile Asn Ala Cys Tyr Asp Ile Thr Ile Asp Ser Met 180 185 190 cca ttt tct cca tat ata tgt gca ggt att ggt agt gac tta gtt tcg 624 Pro Phe Ser Pro Tyr Ile Cys Ala Gly Ile Gly Ser Asp Leu Val Ser 195 200 205 atg ttt gaa act aca aat cct aaa att tct tat caa gga aaa tta ggt 672 Met Phe Glu Thr Thr Asn Pro Lys Ile Ser Tyr Gln Gly Lys Leu Gly 210 215 220 gta agt tac tcc ata agc cca gaa gca tct gtt ttt gtt gga gga cac 720 Val Ser Tyr Ser Ile Ser Pro Glu Ala Ser Val Phe Val Gly Gly His 225 230 235 240 ttt cac aga gtt ata ggt aat gaa ttt aaa gac att cct gca ata act 768 Phe His Arg Val Ile Gly Asn Glu Phe Lys Asp Ile Pro Ala Ile Thr 245 250 255 cct gct gga gca aca gaa att aaa ggc aca cag ttt aca aca gta aca 816 Pro Ala Gly Ala Thr Glu Ile Lys Gly Thr Gln Phe Thr Thr Val Thr 260 265 270 tta aac ata tgc cac ttc gga cta gag ctt gga ggc agg ttt act ttt 864 Leu Asn Ile Cys His Phe Gly Leu Glu Leu Gly Gly Arg Phe Thr Phe 275 280 285 taa 867 32 288 PRT Ehrlichia canis 32 Met Asn Cys Lys Arg Phe Phe Ile Ala Ser Ala Leu Ile Ser Leu Met 1 5 10 15 Ser Phe Leu Pro Ser Val Ser Phe Ser Glu Ser Ile His Glu Asp Asn 20 25 30 Ile Asn Gly Asn Phe Tyr Ile Ser Ala Lys Tyr Met Pro Ser Ala Ser 35 40 45 His Phe Gly Val Phe Ser Val Lys Glu Glu Lys Asn Thr Thr Thr Gly 50 55 60 Val Phe Gly Leu Lys Gln Asp Trp Asp Gly Ala Thr Ile Lys Asp Ala 65 70 75 80 Ser Ser Ser His Thr Ile Asp Pro Ser Thr Ile Phe Ser Ile Ser Asn 85 90 95 Tyr Ser Phe Lys Tyr Glu Asn Asn Pro Phe Leu Gly Phe Ala Gly Ala 100 105 110 Ile Gly Tyr Ser Met Gly Gly Pro Arg Val Glu Phe Glu Val Ser Tyr 115 120 125 Glu Ile Phe Asp Val Lys Asn Gln Gly Asn Ser Tyr Lys Asn Asp Ala 130 135 140 His Lys Tyr Cys Ala Leu Ser Arg His Thr Gly Gly Met Pro Gln Ala 145 150 155 160 Gly His Gln Asn Lys Phe Val Phe Leu Lys Asn Glu Gly Leu Leu Asp 165 170 175 Ile Ser Leu Met Ile Asn Ala Cys Tyr Asp Ile Thr Ile Asp Ser Met 180 185 190 Pro Phe Ser Pro Tyr Ile Cys Ala Gly Ile Gly Ser Asp Leu Val Ser 195 200 205 Met Phe Glu Thr Thr Asn Pro Lys Ile Ser Tyr Gln Gly Lys Leu Gly 210 215 220 Val Ser Tyr Ser Ile Ser Pro Glu Ala Ser Val Phe Val Gly Gly His 225 230 235 240 Phe His Arg Val Ile Gly Asn Glu Phe Lys Asp Ile Pro Ala Ile Thr 245 250 255 Pro Ala Gly Ala Thr Glu Ile Lys Gly Thr Gln Phe Thr Thr Val Thr 260 265 270 Leu Asn Ile Cys His Phe Gly Leu Glu Leu Gly Gly Arg Phe Thr Phe 275 280 285 33 864 DNA Ehrlichia chaffeensis CDS (1)..(864) 33 atg aaa tat aaa aaa act ttt aca gta act gca tta gta tta tta act 48 Met Lys Tyr Lys Lys Thr Phe Thr Val Thr Ala Leu Val Leu Leu Thr 1 5 10 15 tcc ttt aca cat ttt ata cct ttt tat agt cca gca cgt gcc agt aca 96 Ser Phe Thr His Phe Ile Pro Phe Tyr Ser Pro Ala Arg Ala Ser Thr 20 25 30 att cac aac ttc tac att agt gga aaa tat atg cca aca gcg tca cat 144 Ile His Asn Phe Tyr Ile Ser Gly Lys Tyr Met Pro Thr Ala Ser His 35 40 45 ttt gga att ttt tca gct aaa gaa gaa caa agt ttt act aag gta tta 192 Phe Gly Ile Phe Ser Ala Lys Glu Glu Gln Ser Phe Thr Lys Val Leu 50 55 60 gtt ggg tta gat caa cga tta tca cat aat att ata aac aat aat gat 240 Val Gly Leu Asp Gln Arg Leu Ser His Asn Ile Ile Asn Asn Asn Asp 65 70 75 80 aca gca aag agt ctt aag gtt caa aat tat tca ttt aaa tac aaa aat 288 Thr Ala Lys Ser Leu Lys Val Gln Asn Tyr Ser Phe Lys Tyr Lys Asn 85 90 95 aac cca ttt cta gga ttt gca aga gct att ggt tat tca ata ggc aat 336 Asn Pro Phe Leu Gly Phe Ala Arg Ala Ile Gly Tyr Ser Ile Gly Asn 100 105 110 tca aga ata gaa cta gaa gta tca cat gaa ata ttt gat act aaa aac 384 Ser Arg Ile Glu Leu Glu Val Ser His Glu Ile Phe Asp Thr Lys Asn 115 120 125 cca gga aac aat tat tta aat gac tct cac aaa tat tgc gct tta tct 432 Pro Gly Asn Asn Tyr Leu Asn Asp Ser His Lys Tyr Cys Ala Leu Ser 130 135 140 cat gga agt cac ata tgc agt gat gga aat agc gga gat tgg tac act 480 His Gly Ser His Ile Cys Ser Asp Gly Asn Ser Gly Asp Trp Tyr Thr 145 150 155 160 gca aaa act gat aag ttt gta ctt ctg aaa aat gaa ggt tta ctt gac 528 Ala Lys Thr Asp Lys Phe Val Leu Leu Lys Asn Glu Gly Leu Leu Asp 165 170 175 gtc tca ttt atg tta aac gca tgt tat gac ata aca act gaa aaa atg 576 Val Ser Phe Met Leu Asn Ala Cys Tyr Asp Ile Thr Thr Glu Lys Met 180 185 190 cct ttt tca cct tat ata tgt gca ggt att ggt act gat ctc ata tct 624 Pro Phe Ser Pro Tyr Ile Cys Ala Gly Ile Gly Thr Asp Leu Ile Ser 195 200 205 atg ttt gag aca aca caa aac aaa ata tct tat caa gga aag tta ggt 672 Met Phe Glu Thr Thr Gln Asn Lys Ile Ser Tyr Gln Gly Lys Leu Gly 210 215 220 tta aac tat act ata aac tca aga gtt tct gtt ttt gca ggt ggg cac 720 Leu Asn Tyr Thr Ile Asn Ser Arg Val Ser Val Phe Ala Gly Gly His 225 230 235 240 ttt cat aaa gta ata ggt aat gaa ttt aaa ggt att cct act cta tta 768 Phe His Lys Val Ile Gly Asn Glu Phe Lys Gly Ile Pro Thr Leu Leu 245 250 255 cct gat gga tca aac att aaa gta caa cag tct gca aca gta aca tta 816 Pro Asp Gly Ser Asn Ile Lys Val Gln Gln Ser Ala Thr Val Thr Leu 260 265 270 gat gtg tgc cat ttc ggg tta gag att gga agt aga ttt ttc ttt taa 864 Asp Val Cys His Phe Gly Leu Glu Ile Gly Ser Arg Phe Phe Phe 275 280 285 34 287 PRT Ehrlichia chaffeensis 34 Met Lys Tyr Lys Lys Thr Phe Thr Val Thr Ala Leu Val Leu Leu Thr 1 5 10 15 Ser Phe Thr His Phe Ile Pro Phe Tyr Ser Pro Ala Arg Ala Ser Thr 20 25 30 Ile His Asn Phe Tyr Ile Ser Gly Lys Tyr Met Pro Thr Ala Ser His 35 40 45 Phe Gly Ile Phe Ser Ala Lys Glu Glu Gln Ser Phe Thr Lys Val Leu 50 55 60 Val Gly Leu Asp Gln Arg Leu Ser His Asn Ile Ile Asn Asn Asn Asp 65 70 75 80 Thr Ala Lys Ser Leu Lys Val Gln Asn Tyr Ser Phe Lys Tyr Lys Asn 85 90 95 Asn Pro Phe Leu Gly Phe Ala Arg Ala Ile Gly Tyr Ser Ile Gly Asn 100 105 110 Ser Arg Ile Glu Leu Glu Val Ser His Glu Ile Phe Asp Thr Lys Asn 115 120 125 Pro Gly Asn Asn Tyr Leu Asn Asp Ser His Lys Tyr Cys Ala Leu Ser 130 135 140 His Gly Ser His Ile Cys Ser Asp Gly Asn Ser Gly Asp Trp Tyr Thr 145 150 155 160 Ala Lys Thr Asp Lys Phe Val Leu Leu Lys Asn Glu Gly Leu Leu Asp 165 170 175 Val Ser Phe Met Leu Asn Ala Cys Tyr Asp Ile Thr Thr Glu Lys Met 180 185 190 Pro Phe Ser Pro Tyr Ile Cys Ala Gly Ile Gly Thr Asp Leu Ile Ser 195 200 205 Met Phe Glu Thr Thr Gln Asn Lys Ile Ser Tyr Gln Gly Lys Leu Gly 210 215 220 Leu Asn Tyr Thr Ile Asn Ser Arg Val Ser Val Phe Ala Gly Gly His 225 230 235 240 Phe His Lys Val Ile Gly Asn Glu Phe Lys Gly Ile Pro Thr Leu Leu 245 250 255 Pro Asp Gly Ser Asn Ile Lys Val Gln Gln Ser Ala Thr Val Thr Leu 260 265 270 Asp Val Cys His Phe Gly Leu Glu Ile Gly Ser Arg Phe Phe Phe 275 280 285 35 924 DNA Ehrlichia canis CDS (1)..(924) 35 atg ttt tat act aat ata tat att ctg gct tgt att tac ttt gca ctt 48 Met Phe Tyr Thr Asn Ile Tyr Ile Leu Ala Cys Ile Tyr Phe Ala Leu 1 5 10 15 cca cta ttg tta att tat ttt cac tat ttt agg tgt aat atg aat tgc 96 Pro Leu Leu Leu Ile Tyr Phe His Tyr Phe Arg Cys Asn Met Asn Cys 20 25 30 aaa aaa att ctt ata aca act gca tta ata tca tta atg tac tct att 144 Lys Lys Ile Leu Ile Thr Thr Ala Leu Ile Ser Leu Met Tyr Ser Ile 35 40 45 cca agc ata tct ttt tct gat act ata caa gat ggt aac atg ggt ggt 192 Pro Ser Ile Ser Phe Ser Asp Thr Ile Gln Asp Gly Asn Met Gly Gly 50 55 60 aac ttc tat att agt gga aag tat gta cca agt gtc tca cat ttt ggt 240 Asn Phe Tyr Ile Ser Gly Lys Tyr Val Pro Ser Val Ser His Phe Gly 65 70 75 80 agc ttc tca gct aaa gaa gaa agc aaa tca act gtt gga gtt ttt gga 288 Ser Phe Ser Ala Lys Glu Glu Ser Lys Ser Thr Val Gly Val Phe Gly 85 90 95 tta aaa cat gat tgg gat gga agt cca ata ctt aag aat aaa cac gct 336 Leu Lys His Asp Trp Asp Gly Ser Pro Ile Leu Lys Asn Lys His Ala 100 105 110 gac ttt act gtt cca aac tat tcg ttc aga tac gag aac aat cca ttt 384 Asp Phe Thr Val Pro Asn Tyr Ser Phe Arg Tyr Glu Asn Asn Pro Phe 115 120 125 cta ggg ttt gca gga gct atc ggt tac tca atg ggt ggc cca aga ata 432 Leu Gly Phe Ala Gly Ala Ile Gly Tyr Ser Met Gly Gly Pro Arg Ile 130 135 140 gaa ttc gaa ata tct tat gaa gca ttc gac gta aaa agt cct aat atc 480 Glu Phe Glu Ile Ser Tyr Glu Ala Phe Asp Val Lys Ser Pro Asn Ile 145 150 155 160 aat tat caa aat gac gcg cac agg tac tgc gct cta tct cat cac aca 528 Asn Tyr Gln Asn Asp Ala His Arg Tyr Cys Ala Leu Ser His His Thr 165 170 175 tcg gca gcc atg gaa gct gat aaa ttt gtc ttc tta aaa aac gaa ggg 576 Ser Ala Ala Met Glu Ala Asp Lys Phe Val Phe Leu Lys Asn Glu Gly 180 185 190 tta att gac ata tca ctt gca ata aat gca tgt tat gat ata ata aat 624 Leu Ile Asp Ile Ser Leu Ala Ile Asn Ala Cys Tyr Asp Ile Ile Asn 195 200 205 gac aaa gta cct gtt tct cct tat ata tgc gca ggt att ggt act gat 672 Asp Lys Val Pro Val Ser Pro Tyr Ile Cys Ala Gly Ile Gly Thr Asp 210 215 220 ttg att tct atg ttt gaa gct aca agt cct aaa att tcc tac caa gga 720 Leu Ile Ser Met Phe Glu Ala Thr Ser Pro Lys Ile Ser Tyr Gln Gly 225 230 235 240 aaa ctg ggc att agt tac tct att aat ccg gaa acc tct gtt ttc atc 768 Lys Leu Gly Ile Ser Tyr Ser Ile Asn Pro Glu Thr Ser Val Phe Ile 245 250 255 ggt ggg cat ttc cac agg atc ata ggt aat gag ttt aga gat att cct 816 Gly Gly His Phe His Arg Ile Ile Gly Asn Glu Phe Arg Asp Ile Pro 260 265 270 gca ata gta cct agt aac tca act aca ata agt gga cca caa ttt gca 864 Ala Ile Val Pro Ser Asn Ser Thr Thr Ile Ser Gly Pro Gln Phe Ala 275 280 285 aca gta aca cta aat gtg tgt cac ttt ggt tta gaa ctt gga gga aga 912 Thr Val Thr Leu Asn Val Cys His Phe Gly Leu Glu Leu Gly Gly Arg 290 295 300 ttt aac ttc taa 924 Phe Asn Phe 305 36 307 PRT Ehrlichia canis 36 Met Phe Tyr Thr Asn Ile Tyr Ile Leu Ala Cys Ile Tyr Phe Ala Leu 1 5 10 15 Pro Leu Leu Leu Ile Tyr Phe His Tyr Phe Arg Cys Asn Met Asn Cys 20 25 30 Lys Lys Ile Leu Ile Thr Thr Ala Leu Ile Ser Leu Met Tyr Ser Ile 35 40 45 Pro Ser Ile Ser Phe Ser Asp Thr Ile Gln Asp Gly Asn Met Gly Gly 50 55 60 Asn Phe Tyr Ile Ser Gly Lys Tyr Val Pro Ser Val Ser His Phe Gly 65 70 75 80 Ser Phe Ser Ala Lys Glu Glu Ser Lys Ser Thr Val Gly Val Phe Gly 85 90 95 Leu Lys His Asp Trp Asp Gly Ser Pro Ile Leu Lys Asn Lys His Ala 100 105 110 Asp Phe Thr Val Pro Asn Tyr Ser Phe Arg Tyr Glu Asn Asn Pro Phe 115 120 125 Leu Gly Phe Ala Gly Ala Ile Gly Tyr Ser Met Gly Gly Pro Arg Ile 130 135 140 Glu Phe Glu Ile Ser Tyr Glu Ala Phe Asp Val Lys Ser Pro Asn Ile 145 150 155 160 Asn Tyr Gln Asn Asp Ala His Arg Tyr Cys Ala Leu Ser His His Thr 165 170 175 Ser Ala Ala Met Glu Ala Asp Lys Phe Val Phe Leu Lys Asn Glu Gly 180 185 190 Leu Ile Asp Ile Ser Leu Ala Ile Asn Ala Cys Tyr Asp Ile Ile Asn 195 200 205 Asp Lys Val Pro Val Ser Pro Tyr Ile Cys Ala Gly Ile Gly Thr Asp 210 215 220 Leu Ile Ser Met Phe Glu Ala Thr Ser Pro Lys Ile Ser Tyr Gln Gly 225 230 235 240 Lys Leu Gly Ile Ser Tyr Ser Ile Asn Pro Glu Thr Ser Val Phe Ile 245 250 255 Gly Gly His Phe His Arg Ile Ile Gly Asn Glu Phe Arg Asp Ile Pro 260 265 270 Ala Ile Val Pro Ser Asn Ser Thr Thr Ile Ser Gly Pro Gln Phe Ala 275 280 285 Thr Val Thr Leu Asn Val Cys His Phe Gly Leu Glu Leu Gly Gly Arg 290 295 300 Phe Asn Phe 305 37 843 DNA Ehrlichia canis CDS (1)..(843) 37 atg aat tgc aaa aaa att ctt ata aca act gca tta atg tca tta atg 48 Met Asn Cys Lys Lys Ile Leu Ile Thr Thr Ala Leu Met Ser Leu Met 1 5 10 15 tac tat gct cca agc ata tct ttt tct gat act ata caa gac gat aac 96 Tyr Tyr Ala Pro Ser Ile Ser Phe Ser Asp Thr Ile Gln Asp Asp Asn 20 25 30 act ggt agc ttc tac atc agt gga aaa tat gta cca agt gtt tca cat 144 Thr Gly Ser Phe Tyr Ile Ser Gly Lys Tyr Val Pro Ser Val Ser His 35 40 45 ttt ggt gtt ttc tca gct aaa gaa gaa aga aac tca act gtt gga gtt 192 Phe Gly Val Phe Ser Ala Lys Glu Glu Arg Asn Ser Thr Val Gly Val 50 55 60 ttt gga tta aaa cat gat tgg aat gga ggt aca ata tct aac tct tct 240 Phe Gly Leu Lys His Asp Trp Asn Gly Gly Thr Ile Ser Asn Ser Ser 65 70 75 80 cca gaa aat ata ttc aca gtt caa aat tat tcg ttt aaa tac gaa aac 288 Pro Glu Asn Ile Phe Thr Val Gln Asn Tyr Ser Phe Lys Tyr Glu Asn 85 90 95 aac cca ttc tta ggg ttt gca gga gct att ggt tat tca atg ggt ggc 336 Asn Pro Phe Leu Gly Phe Ala Gly Ala Ile Gly Tyr Ser Met Gly Gly 100 105 110 cca aga ata gaa ctt gaa gtt ctg tac gag aca ttc gat gtg aaa aat 384 Pro Arg Ile Glu Leu Glu Val Leu Tyr Glu Thr Phe Asp Val Lys Asn 115 120 125 cag aac aat aat tat aag aac ggc gca cac aga tac tgt gct tta tct 432 Gln Asn Asn Asn Tyr Lys Asn Gly Ala His Arg Tyr Cys Ala Leu Ser 130 135 140 cat cat agt tca gca aca aac atg tcc tcc gca agt aac aaa ttt gtt 480 His His Ser Ser Ala Thr Asn Met Ser Ser Ala Ser Asn Lys Phe Val 145 150 155 160 ttc tta aaa aat gaa ggg tta att gac tta tca ttt atg ata aat gca 528 Phe Leu Lys Asn Glu Gly Leu Ile Asp Leu Ser Phe Met Ile Asn Ala 165 170 175 tgc tat gac ata ata att gaa gga atg cct ttt tca cct tat att tgt 576 Cys Tyr Asp Ile Ile Ile Glu Gly Met Pro Phe Ser Pro Tyr Ile Cys 180 185 190 gca ggt gtt ggt act gat gtt gtt tcc atg ttt gaa gct ata aat cct 624 Ala Gly Val Gly Thr Asp Val Val Ser Met Phe Glu Ala Ile Asn Pro 195 200 205 aaa att tct tac caa gga aaa cta gga tta ggt tat agt ata agt tca 672 Lys Ile Ser Tyr Gln Gly Lys Leu Gly Leu Gly Tyr Ser Ile Ser Ser 210 215 220 gaa gcc tct gtt ttt atc ggt gga cac ttt cac aga gtc ata ggt aat 720 Glu Ala Ser Val Phe Ile Gly Gly His Phe His Arg Val Ile Gly Asn 225 230 235 240 gaa ttt aga gac atc cct gct atg gtt cct agt gga tca aat ctt cca 768 Glu Phe Arg Asp Ile Pro Ala Met Val Pro Ser Gly Ser Asn Leu Pro 245 250 255 gaa aac caa ttt gca ata gta aca cta aat gtg tgt cac ttt ggt tta 816 Glu Asn Gln Phe Ala Ile Val Thr Leu Asn Val Cys His Phe Gly Leu 260 265 270 gaa ctt gga gga aga ttt aac ttc tga 843 Glu Leu Gly Gly Arg Phe Asn Phe 275 280 38 280 PRT Ehrlichia canis 38 Met Asn Cys Lys Lys Ile Leu Ile Thr Thr Ala Leu Met Ser Leu Met 1 5 10 15 Tyr Tyr Ala Pro Ser Ile Ser Phe Ser Asp Thr Ile Gln Asp Asp Asn 20 25 30 Thr Gly Ser Phe Tyr Ile Ser Gly Lys Tyr Val Pro Ser Val Ser His 35 40 45 Phe Gly Val Phe Ser Ala Lys Glu Glu Arg Asn Ser Thr Val Gly Val 50 55 60 Phe Gly Leu Lys His Asp Trp Asn Gly Gly Thr Ile Ser Asn Ser Ser 65 70 75 80 Pro Glu Asn Ile Phe Thr Val Gln Asn Tyr Ser Phe Lys Tyr Glu Asn 85 90 95 Asn Pro Phe Leu Gly Phe Ala Gly Ala Ile Gly Tyr Ser Met Gly Gly 100 105 110 Pro Arg Ile Glu Leu Glu Val Leu Tyr Glu Thr Phe Asp Val Lys Asn 115 120 125 Gln Asn Asn Asn Tyr Lys Asn Gly Ala His Arg Tyr Cys Ala Leu Ser 130 135 140 His His Ser Ser Ala Thr Asn Met Ser Ser Ala Ser Asn Lys Phe Val 145 150 155 160 Phe Leu Lys Asn Glu Gly Leu Ile Asp Leu Ser Phe Met Ile Asn Ala 165 170 175 Cys Tyr Asp Ile Ile Ile Glu Gly Met Pro Phe Ser Pro Tyr Ile Cys 180 185 190 Ala Gly Val Gly Thr Asp Val Val Ser Met Phe Glu Ala Ile Asn Pro 195 200 205 Lys Ile Ser Tyr Gln Gly Lys Leu Gly Leu Gly Tyr Ser Ile Ser Ser 210 215 220 Glu Ala Ser Val Phe Ile Gly Gly His Phe His Arg Val Ile Gly Asn 225 230 235 240 Glu Phe Arg Asp Ile Pro Ala Met Val Pro Ser Gly Ser Asn Leu Pro 245 250 255 Glu Asn Gln Phe Ala Ile Val Thr Leu Asn Val Cys His Phe Gly Leu 260 265 270 Glu Leu Gly Gly Arg Phe Asn Phe 275 280 39 852 DNA Ehrlichia canis CDS (1)..(852) 39 atg aat tgt aaa aaa gtt ttc aca ata agt gca ttg ata tca tcc ata 48 Met Asn Cys Lys Lys Val Phe Thr Ile Ser Ala Leu Ile Ser Ser Ile 1 5 10 15 tac ttc cta cct aat gtc tca tac tct aac cca gta tat ggt aac agt 96 Tyr Phe Leu Pro Asn Val Ser Tyr Ser Asn Pro Val Tyr Gly Asn Ser 20 25 30 atg tat ggt aat ttt tac ata tca gga aag tac atg cca agt gtt cct 144 Met Tyr Gly Asn Phe Tyr Ile Ser Gly Lys Tyr Met Pro Ser Val Pro 35 40 45 cat ttt gga att ttt tca gct gaa gaa gag aaa aaa aag aca act gta 192 His Phe Gly Ile Phe Ser Ala Glu Glu Glu Lys Lys Lys Thr Thr Val 50 55 60 gta tat ggc tta aaa gga aaa ctg gca gga gat gca ata tct agt caa 240 Val Tyr Gly Leu Lys Gly Lys Leu Ala Gly Asp Ala Ile Ser Ser Gln 65 70 75 80 agt cca gat gat aat ttt acc att cga aat tac tca ttc aag tat gca 288 Ser Pro Asp Asp Asn Phe Thr Ile Arg Asn Tyr Ser Phe Lys Tyr Ala 85 90 95 agc aac aag ttt tta ggg ttt gca gta gct att ggt tac tcg ata ggc 336 Ser Asn Lys Phe Leu Gly Phe Ala Val Ala Ile Gly Tyr Ser Ile Gly 100 105 110 agt cca aga ata gaa gtt gag atg tct tat gaa gca ttt gat gtg aaa 384 Ser Pro Arg Ile Glu Val Glu Met Ser Tyr Glu Ala Phe Asp Val Lys 115 120 125 aat cca ggt gat aat tac aaa aac ggt gct tac agg tat tgt gct tta 432 Asn Pro Gly Asp Asn Tyr Lys Asn Gly Ala Tyr Arg Tyr Cys Ala Leu 130 135 140 tct cat caa gat gat gcg gat gat gac atg act agt gca act gac aaa 480 Ser His Gln Asp Asp Ala Asp Asp Asp Met Thr Ser Ala Thr Asp Lys 145 150 155 160 ttt gta tat tta att aat gaa gga tta ctt aac ata tca ttt atg aca 528 Phe Val Tyr Leu Ile Asn Glu Gly Leu Leu Asn Ile Ser Phe Met Thr 165 170 175 aac ata tgt tat gaa aca gca agc aaa aat ata cct ctc tct cct tac 576 Asn Ile Cys Tyr Glu Thr Ala Ser Lys Asn Ile Pro Leu Ser Pro Tyr 180 185 190 ata tgt gca ggt att ggt act gat tta att cac atg ttt gaa act aca 624 Ile Cys Ala Gly Ile Gly Thr Asp Leu Ile His Met Phe Glu Thr Thr 195 200 205 cat cct aaa att tct tat caa gga aag cta ggg ttg gcc tac ttc gta 672 His Pro Lys Ile Ser Tyr Gln Gly Lys Leu Gly Leu Ala Tyr Phe Val 210 215 220 agt gca gag tct tcg gtt tct ttt ggt ata tat ttt cat aaa att ata 720 Ser Ala Glu Ser Ser Val Ser Phe Gly Ile Tyr Phe His Lys Ile Ile 225 230 235 240 aat aat aag ttt aaa aat gtt cca gcc atg gta cct att aac tca gac 768 Asn Asn Lys Phe Lys Asn Val Pro Ala Met Val Pro Ile Asn Ser Asp 245 250 255 gag ata gta gga cca cag ttt gca aca gta aca tta aat gta tgc tac 816 Glu Ile Val Gly Pro Gln Phe Ala Thr Val Thr Leu Asn Val Cys Tyr 260 265 270 ttt gga tta gaa ctt gga tgt agg ttc aac ttc taa 852 Phe Gly Leu Glu Leu Gly Cys Arg Phe Asn Phe 275 280 40 283 PRT Ehrlichia canis 40 Met Asn Cys Lys Lys Val Phe Thr Ile Ser Ala Leu Ile Ser Ser Ile 1 5 10 15 Tyr Phe Leu Pro Asn Val Ser Tyr Ser Asn Pro Val Tyr Gly Asn Ser 20 25 30 Met Tyr Gly Asn Phe Tyr Ile Ser Gly Lys Tyr Met Pro Ser Val Pro 35 40 45 His Phe Gly Ile Phe Ser Ala Glu Glu Glu Lys Lys Lys Thr Thr Val 50 55 60 Val Tyr Gly Leu Lys Gly Lys Leu Ala Gly Asp Ala Ile Ser Ser Gln 65 70 75 80 Ser Pro Asp Asp Asn Phe Thr Ile Arg Asn Tyr Ser Phe Lys Tyr Ala 85 90 95 Ser Asn Lys Phe Leu Gly Phe Ala Val Ala Ile Gly Tyr Ser Ile Gly 100 105 110 Ser Pro Arg Ile Glu Val Glu Met Ser Tyr Glu Ala Phe Asp Val Lys 115 120 125 Asn Pro Gly Asp Asn Tyr Lys Asn Gly Ala Tyr Arg Tyr Cys Ala Leu 130 135 140 Ser His Gln Asp Asp Ala Asp Asp Asp Met Thr Ser Ala Thr Asp Lys 145 150 155 160 Phe Val Tyr Leu Ile Asn Glu Gly Leu Leu Asn Ile Ser Phe Met Thr 165 170 175 Asn Ile Cys Tyr Glu Thr Ala Ser Lys Asn Ile Pro Leu Ser Pro Tyr 180 185 190 Ile Cys Ala Gly Ile Gly Thr Asp Leu Ile His Met Phe Glu Thr Thr 195 200 205 His Pro Lys Ile Ser Tyr Gln Gly Lys Leu Gly Leu Ala Tyr Phe Val 210 215 220 Ser Ala Glu Ser Ser Val Ser Phe Gly Ile Tyr Phe His Lys Ile Ile 225 230 235 240 Asn Asn Lys Phe Lys Asn Val Pro Ala Met Val Pro Ile Asn Ser Asp 245 250 255 Glu Ile Val Gly Pro Gln Phe Ala Thr Val Thr Leu Asn Val Cys Tyr 260 265 270 Phe Gly Leu Glu Leu Gly Cys Arg Phe Asn Phe 275 280 41 831 DNA Ehrlichia canis CDS (1)..(831) 41 atg aac tgt aaa aaa ttt ctt ata aca act aca ttg gta tca cta aca 48 Met Asn Cys Lys Lys Phe Leu Ile Thr Thr Thr Leu Val Ser Leu Thr 1 5 10 15 att ctt tta cct ggc ata tct ttc tcc aaa cca ata cat gaa aac aat 96 Ile Leu Leu Pro Gly Ile Ser Phe Ser Lys Pro Ile His Glu Asn Asn 20 25 30 act aca gga aac ttt tac att att gga aaa tat gta cca agt att tca 144 Thr Thr Gly Asn Phe Tyr Ile Ile Gly Lys Tyr Val Pro Ser Ile Ser 35 40 45 cat ttt ggg aac ttt tca gct aaa gaa gaa aaa aac aca act act gga 192 His Phe Gly Asn Phe Ser Ala Lys Glu Glu Lys Asn Thr Thr Thr Gly 50 55 60 att ttt gga tta aaa gaa tca tgg act ggt ggt atc atc ctt gat aaa 240 Ile Phe Gly Leu Lys Glu Ser Trp Thr Gly Gly Ile Ile Leu Asp Lys 65 70 75 80 gaa cat gca gct ttt aat atc cca aat tat tca ttt aaa tat gaa aat 288 Glu His Ala Ala Phe Asn Ile Pro Asn Tyr Ser Phe Lys Tyr Glu Asn 85 90 95 aat cca ttt tta gga ttt gca ggg gta att ggc tat tca ata ggt agt 336 Asn Pro Phe Leu Gly Phe Ala Gly Val Ile Gly Tyr Ser Ile Gly Ser 100 105 110 cca aga ata gaa ttt gaa gta tca tac gag aca ttc gat gta caa aat 384 Pro Arg Ile Glu Phe Glu Val Ser Tyr Glu Thr Phe Asp Val Gln Asn 115 120 125 cca gga gat aag ttt aac aat gat gca cat aag tat tgt gct tta tcc 432 Pro Gly Asp Lys Phe Asn Asn Asp Ala His Lys Tyr Cys Ala Leu Ser 130 135 140 aat gat tcc agt aaa aca atg aaa agt ggt aaa ttc gtt ttt ctc aaa 480 Asn Asp Ser Ser Lys Thr Met Lys Ser Gly Lys Phe Val Phe Leu Lys 145 150 155 160 aat gaa gga tta agt gac ata tca ctc atg tta aat gta tgt tat gat 528 Asn Glu Gly Leu Ser Asp Ile Ser Leu Met Leu Asn Val Cys Tyr Asp 165 170 175 ata ata aac aaa aga atg cct ttt tca cct tac ata tgt gca ggc att 576 Ile Ile Asn Lys Arg Met Pro Phe Ser Pro Tyr Ile Cys Ala Gly Ile 180 185 190 ggt act gac tta ata ttc atg ttt gac gct ata aac cat aaa gct gct 624 Gly Thr Asp Leu Ile Phe Met Phe Asp Ala Ile Asn His Lys Ala Ala 195 200 205 tat caa gga aaa tta ggt ttt aat tat cca ata agc cca gaa gct aac 672 Tyr Gln Gly Lys Leu Gly Phe Asn Tyr Pro Ile Ser Pro Glu Ala Asn 210 215 220 att tct atg ggt gtg cac ttt cac aaa gta aca aac aac gag ttt aga 720 Ile Ser Met Gly Val His Phe His Lys Val Thr Asn Asn Glu Phe Arg 225 230 235 240 gtt cct gtt cta tta act gct gga gga ctc gct cca gat aat cta ttt 768 Val Pro Val Leu Leu Thr Ala Gly Gly Leu Ala Pro Asp Asn Leu Phe 245 250 255 gca ata gta aag ttg agt ata tgt cat ttt ggg tta gaa ttt ggg tac 816 Ala Ile Val Lys Leu Ser Ile Cys His Phe Gly Leu Glu Phe Gly Tyr 260 265 270 agg gtc agt ttt taa 831 Arg Val Ser Phe 275 42 276 PRT Ehrlichia canis 42 Met Asn Cys Lys Lys Phe Leu Ile Thr Thr Thr Leu Val Ser Leu Thr 1 5 10 15 Ile Leu Leu Pro Gly Ile Ser Phe Ser Lys Pro Ile His Glu Asn Asn 20 25 30 Thr Thr Gly Asn Phe Tyr Ile Ile Gly Lys Tyr Val Pro Ser Ile Ser 35 40 45 His Phe Gly Asn Phe Ser Ala Lys Glu Glu Lys Asn Thr Thr Thr Gly 50 55 60 Ile Phe Gly Leu Lys Glu Ser Trp Thr Gly Gly Ile Ile Leu Asp Lys 65 70 75 80 Glu His Ala Ala Phe Asn Ile Pro Asn Tyr Ser Phe Lys Tyr Glu Asn 85 90 95 Asn Pro Phe Leu Gly Phe Ala Gly Val Ile Gly Tyr Ser Ile Gly Ser 100 105 110 Pro Arg Ile Glu Phe Glu Val Ser Tyr Glu Thr Phe Asp Val Gln Asn 115 120 125 Pro Gly Asp Lys Phe Asn Asn Asp Ala His Lys Tyr Cys Ala Leu Ser 130 135 140 Asn Asp Ser Ser Lys Thr Met Lys Ser Gly Lys Phe Val Phe Leu Lys 145 150 155 160 Asn Glu Gly Leu Ser Asp Ile Ser Leu Met Leu Asn Val Cys Tyr Asp 165 170 175 Ile Ile Asn Lys Arg Met Pro Phe Ser Pro Tyr Ile Cys Ala Gly Ile 180 185 190 Gly Thr Asp Leu Ile Phe Met Phe Asp Ala Ile Asn His Lys Ala Ala 195 200 205 Tyr Gln Gly Lys Leu Gly Phe Asn Tyr Pro Ile Ser Pro Glu Ala Asn 210 215 220 Ile Ser Met Gly Val His Phe His Lys Val Thr Asn Asn Glu Phe Arg 225 230 235 240 Val Pro Val Leu Leu Thr Ala Gly Gly Leu Ala Pro Asp Asn Leu Phe 245 250 255 Ala Ile Val Lys Leu Ser Ile Cys His Phe Gly Leu Glu Phe Gly Tyr 260 265 270 Arg Val Ser Phe 275 43 882 DNA Ehrlichia canis CDS (1)..(882) 43 atg aat aat aaa ctc aaa ttt act ata ata aac aca gta tta gta tgc 48 Met Asn Asn Lys Leu Lys Phe Thr Ile Ile Asn Thr Val Leu Val Cys 1 5 10 15 tta ttg tca tta cct aat ata tct tcc tca aag gcc ata aac aat aac 96 Leu Leu Ser Leu Pro Asn Ile Ser Ser Ser Lys Ala Ile Asn Asn Asn 20 25 30 gct aaa aag tac tac gga tta tat atc agt gga caa tat aaa ccc agt 144 Ala Lys Lys Tyr Tyr Gly Leu Tyr Ile Ser Gly Gln Tyr Lys Pro Ser 35 40 45 gtt tct gtt ttc agt aat ttt tca gtt aaa gaa acc aat gtc ata act 192 Val Ser Val Phe Ser Asn Phe Ser Val Lys Glu Thr Asn Val Ile Thr 50 55 60 aaa aac ctt ata gct tta aaa aaa gat gtt gac tct att gaa acc aag 240 Lys Asn Leu Ile Ala Leu Lys Lys Asp Val Asp Ser Ile Glu Thr Lys 65 70 75 80 act gat gcc agt gta ggt att agt aac cca tca aat ttt act atc ccc 288 Thr Asp Ala Ser Val Gly Ile Ser Asn Pro Ser Asn Phe Thr Ile Pro 85 90 95 tat aca gct gta ttt caa gat aat tct gtc aat ttc aat gga act att 336 Tyr Thr Ala Val Phe Gln Asp Asn Ser Val Asn Phe Asn Gly Thr Ile 100 105 110 ggt tac acc ttt gct gaa ggt aca aga gtt gaa ata gaa ggt tct tat 384 Gly Tyr Thr Phe Ala Glu Gly Thr Arg Val Glu Ile Glu Gly Ser Tyr 115 120 125 gag gaa ttt gat gtt aaa aac cct gga ggc tat aca cta agt gat gcc 432 Glu Glu Phe Asp Val Lys Asn Pro Gly Gly Tyr Thr Leu Ser Asp Ala 130 135 140 tat cgc tat ttt gca tta gca cgt gaa atg aaa ggt aat agt ttt aca 480 Tyr Arg Tyr Phe Ala Leu Ala Arg Glu Met Lys Gly Asn Ser Phe Thr 145 150 155 160 cct aaa gaa aaa gtt tct aat agt ttt ttt cac act gta atg aga aat 528 Pro Lys Glu Lys Val Ser Asn Ser Phe Phe His Thr Val Met Arg Asn 165 170 175 gat gga tta tct ata ata tct gtt ata gta aat gtt tgc tac gat ttc 576 Asp Gly Leu Ser Ile Ile Ser Val Ile Val Asn Val Cys Tyr Asp Phe 180 185 190 tct ttg aac aat ttg tca ata tcg cct tac ata tgt gga gga gca ggg 624 Ser Leu Asn Asn Leu Ser Ile Ser Pro Tyr Ile Cys Gly Gly Ala Gly 195 200 205 gta gat gct ata gaa ttc ttc gat gta tta cac att aag ttt gca tat 672 Val Asp Ala Ile Glu Phe Phe Asp Val Leu His Ile Lys Phe Ala Tyr 210 215 220 caa agc aag cta ggt att gct tat tct cta cca tct aac att agt ctc 720 Gln Ser Lys Leu Gly Ile Ala Tyr Ser Leu Pro Ser Asn Ile Ser Leu 225 230 235 240 ttt gct agt tta tat tac cat aaa gta atg ggc aat caa ttt aaa aat 768 Phe Ala Ser Leu Tyr Tyr His Lys Val Met Gly Asn Gln Phe Lys Asn 245 250 255 tta aat gtc caa gat gtt gct gaa ctt gca agt ata cct aaa att aca 816 Leu Asn Val Gln Asp Val Ala Glu Leu Ala Ser Ile Pro Lys Ile Thr 260 265 270 tcc gca gtt gct aca ctt aat att ggt tat ttt gga ggt gaa att ggt 864 Ser Ala Val Ala Thr Leu Asn Ile Gly Tyr Phe Gly Gly Glu Ile Gly 275 280 285 gca aga ttg aca ttt taa 882 Ala Arg Leu Thr Phe 290 44 293 PRT Ehrlichia canis 44 Met Asn Asn Lys Leu Lys Phe Thr Ile Ile Asn Thr Val Leu Val Cys 1 5 10 15 Leu Leu Ser Leu Pro Asn Ile Ser Ser Ser Lys Ala Ile Asn Asn Asn 20 25 30 Ala Lys Lys Tyr Tyr Gly Leu Tyr Ile Ser Gly Gln Tyr Lys Pro Ser 35 40 45 Val Ser Val Phe Ser Asn Phe Ser Val Lys Glu Thr Asn Val Ile Thr 50 55 60 Lys Asn Leu Ile Ala Leu Lys Lys Asp Val Asp Ser Ile Glu Thr Lys 65 70 75 80 Thr Asp Ala Ser Val Gly Ile Ser Asn Pro Ser Asn Phe Thr Ile Pro 85 90 95 Tyr Thr Ala Val Phe Gln Asp Asn Ser Val Asn Phe Asn Gly Thr Ile 100 105 110 Gly Tyr Thr Phe Ala Glu Gly Thr Arg Val Glu Ile Glu Gly Ser Tyr 115 120 125 Glu Glu Phe Asp Val Lys Asn Pro Gly Gly Tyr Thr Leu Ser Asp Ala 130 135 140 Tyr Arg Tyr Phe Ala Leu Ala Arg Glu Met Lys Gly Asn Ser Phe Thr 145 150 155 160 Pro Lys Glu Lys Val Ser Asn Ser Phe Phe His Thr Val Met Arg Asn 165 170 175 Asp Gly Leu Ser Ile Ile Ser Val Ile Val Asn Val Cys Tyr Asp Phe 180 185 190 Ser Leu Asn Asn Leu Ser Ile Ser Pro Tyr Ile Cys Gly Gly Ala Gly 195 200 205 Val Asp Ala Ile Glu Phe Phe Asp Val Leu His Ile Lys Phe Ala Tyr 210 215 220 Gln Ser Lys Leu Gly Ile Ala Tyr Ser Leu Pro Ser Asn Ile Ser Leu 225 230 235 240 Phe Ala Ser Leu Tyr Tyr His Lys Val Met Gly Asn Gln Phe Lys Asn 245 250 255 Leu Asn Val Gln Asp Val Ala Glu Leu Ala Ser Ile Pro Lys Ile Thr 260 265 270 Ser Ala Val Ala Thr Leu Asn Ile Gly Tyr Phe Gly Gly Glu Ile Gly 275 280 285 Ala Arg Leu Thr Phe 290 45 900 DNA Ehrlichia canis CDS (1)..(900) 45 atg aat agc aag agt aag ttc ttt aca ata tgt aca tcg tta ata tgc 48 Met Asn Ser Lys Ser Lys Phe Phe Thr Ile Cys Thr Ser Leu Ile Cys 1 5 10 15 tta tta tca tca cct aac aca tct ctc tca aac ttc ata ggc aat agt 96 Leu Leu Ser Ser Pro Asn Thr Ser Leu Ser Asn Phe Ile Gly Asn Ser 20 25 30 aca aaa cat tct gga tta tat gtt agc gga cat tat aag ccc agc gtt 144 Thr Lys His Ser Gly Leu Tyr Val Ser Gly His Tyr Lys Pro Ser Val 35 40 45 tcc att ttt agc aaa ttt tca gta aaa gaa aca aat aca cat aca gta 192 Ser Ile Phe Ser Lys Phe Ser Val Lys Glu Thr Asn Thr His Thr Val 50 55 60 cag tta gta gct ctt aaa aaa gat gtt aat tct att tct atg aac atc 240 Gln Leu Val Ala Leu Lys Lys Asp Val Asn Ser Ile Ser Met Asn Ile 65 70 75 80 agt aat ggt gct aca ggc att agc aaa gca aca aat ttt aat ctt cct 288 Ser Asn Gly Ala Thr Gly Ile Ser Lys Ala Thr Asn Phe Asn Leu Pro 85 90 95 tat gtt gca gaa ttt caa gac aat gcc ttc aac ttc agt gga gct att 336 Tyr Val Ala Glu Phe Gln Asp Asn Ala Phe Asn Phe Ser Gly Ala Ile 100 105 110 ggt tat tca ctt ttt gaa caa cta aac att gaa gtt gaa ggt tct tat 384 Gly Tyr Ser Leu Phe Glu Gln Leu Asn Ile Glu Val Glu Gly Ser Tyr 115 120 125 gaa gaa ttc gat gcc aaa aat cct ggt ggt tat att tta aat gat gca 432 Glu Glu Phe Asp Ala Lys Asn Pro Gly Gly Tyr Ile Leu Asn Asp Ala 130 135 140 ttc cgc tat ttt gca ttg gca cgt gaa atg gga caa gaa aaa aat gat 480 Phe Arg Tyr Phe Ala Leu Ala Arg Glu Met Gly Gln Glu Lys Asn Asp 145 150 155 160 aat aag cat ctt agt cct aag gag gag cat gat ata agt aaa aca tat 528 Asn Lys His Leu Ser Pro Lys Glu Glu His Asp Ile Ser Lys Thr Tyr 165 170 175 tac aca gtc atg aga aat aat ggg tta tct ata tta tct att atg ata 576 Tyr Thr Val Met Arg Asn Asn Gly Leu Ser Ile Leu Ser Ile Met Ile 180 185 190 aat ggc tgc tat aat cta cct ctc aat gat tta tca ata tca cct tat 624 Asn Gly Cys Tyr Asn Leu Pro Leu Asn Asp Leu Ser Ile Ser Pro Tyr 195 200 205 ttt tgt aca gga ata ggt gta gat gct ata gaa ttt ttt gat gca ctg 672 Phe Cys Thr Gly Ile Gly Val Asp Ala Ile Glu Phe Phe Asp Ala Leu 210 215 220 cat ctt aaa ctt gct ttg caa agt aaa ata gga gct act tac caa tta 720 His Leu Lys Leu Ala Leu Gln Ser Lys Ile Gly Ala Thr Tyr Gln Leu 225 230 235 240 tca gac aac att agt tta ttt aca aat gga tat tac cat caa gta ata 768 Ser Asp Asn Ile Ser Leu Phe Thr Asn Gly Tyr Tyr His Gln Val Ile 245 250 255 ggt gat caa ttt aaa aac tta aaa gtc caa tat ata ggt gaa ctt aaa 816 Gly Asp Gln Phe Lys Asn Leu Lys Val Gln Tyr Ile Gly Glu Leu Lys 260 265 270 gag aac ccg aaa att aca tct gca gtt gct act ctc aat gtt gga tac 864 Glu Asn Pro Lys Ile Thr Ser Ala Val Ala Thr Leu Asn Val Gly Tyr 275 280 285 ttt gga ggt gaa att gga gta aga ctc aca ctt taa 900 Phe Gly Gly Glu Ile Gly Val Arg Leu Thr Leu 290 295 300 46 299 PRT Ehrlichia canis 46 Met Asn Ser Lys Ser Lys Phe Phe Thr Ile Cys Thr Ser Leu Ile Cys 1 5 10 15 Leu Leu Ser Ser Pro Asn Thr Ser Leu Ser Asn Phe Ile Gly Asn Ser 20 25 30 Thr Lys His Ser Gly Leu Tyr Val Ser Gly His Tyr Lys Pro Ser Val 35 40 45 Ser Ile Phe Ser Lys Phe Ser Val Lys Glu Thr Asn Thr His Thr Val 50 55 60 Gln Leu Val Ala Leu Lys Lys Asp Val Asn Ser Ile Ser Met Asn Ile 65 70 75 80 Ser Asn Gly Ala Thr Gly Ile Ser Lys Ala Thr Asn Phe Asn Leu Pro 85 90 95 Tyr Val Ala Glu Phe Gln Asp Asn Ala Phe Asn Phe Ser Gly Ala Ile 100 105 110 Gly Tyr Ser Leu Phe Glu Gln Leu Asn Ile Glu Val Glu Gly Ser Tyr 115 120 125 Glu Glu Phe Asp Ala Lys Asn Pro Gly Gly Tyr Ile Leu Asn Asp Ala 130 135 140 Phe Arg Tyr Phe Ala Leu Ala Arg Glu Met Gly Gln Glu Lys Asn Asp 145 150 155 160 Asn Lys His Leu Ser Pro Lys Glu Glu His Asp Ile Ser Lys Thr Tyr 165 170 175 Tyr Thr Val Met Arg Asn Asn Gly Leu Ser Ile Leu Ser Ile Met Ile 180 185 190 Asn Gly Cys Tyr Asn Leu Pro Leu Asn Asp Leu Ser Ile Ser Pro Tyr 195 200 205 Phe Cys Thr Gly Ile Gly Val Asp Ala Ile Glu Phe Phe Asp Ala Leu 210 215 220 His Leu Lys Leu Ala Leu Gln Ser Lys Ile Gly Ala Thr Tyr Gln Leu 225 230 235 240 Ser Asp Asn Ile Ser Leu Phe Thr Asn Gly Tyr Tyr His Gln Val Ile 245 250 255 Gly Asp Gln Phe Lys Asn Leu Lys Val Gln Tyr Ile Gly Glu Leu Lys 260 265 270 Glu Asn Pro Lys Ile Thr Ser Ala Val Ala Thr Leu Asn Val Gly Tyr 275 280 285 Phe Gly Gly Glu Ile Gly Val Arg Leu Thr Leu 290 295 47 843 DNA Ehrlichia canis CDS (1)..(843) 47 atg aat tat aag aaa att cta gta aga agc gcg tta atc tca tta atg 48 Met Asn Tyr Lys Lys Ile Leu Val Arg Ser Ala Leu Ile Ser Leu Met 1 5 10 15 tca atc tta cca tat cag tct ttt gca gat cct gta ggt tca aga act 96 Ser Ile Leu Pro Tyr Gln Ser Phe Ala Asp Pro Val Gly Ser Arg Thr 20 25 30 aat gat aac aaa gaa ggc ttc tac att agt gca aag tac aat cca agt 144 Asn Asp Asn Lys Glu Gly Phe Tyr Ile Ser Ala Lys Tyr Asn Pro Ser 35 40 45 ata tca cac ttt aga aaa ttc tct gct gaa gaa act cct att aat gga 192 Ile Ser His Phe Arg Lys Phe Ser Ala Glu Glu Thr Pro Ile Asn Gly 50 55 60 aca aat tct ctc act aaa aaa gtt ttc gga cta aag aaa gat ggt gat 240 Thr Asn Ser Leu Thr Lys Lys Val Phe Gly Leu Lys Lys Asp Gly Asp 65 70 75 80 ata aca aaa aaa gac gat ttt aca aga gta gct cca ggc att gat ttt 288 Ile Thr Lys Lys Asp Asp Phe Thr Arg Val Ala Pro Gly Ile Asp Phe 85 90 95 caa aat aac tta ata tca gga ttt tca gga agt att ggt tac tct atg 336 Gln Asn Asn Leu Ile Ser Gly Phe Ser Gly Ser Ile Gly Tyr Ser Met 100 105 110 gac gga cca aga ata gaa ctt gaa gct gca tat caa caa ttt aat cca 384 Asp Gly Pro Arg Ile Glu Leu Glu Ala Ala Tyr Gln Gln Phe Asn Pro 115 120 125 aaa aac acc gat aac aat gat act gat aat ggt gaa tac tat aaa cat 432 Lys Asn Thr Asp Asn Asn Asp Thr Asp Asn Gly Glu Tyr Tyr Lys His 130 135 140 ttt gca tta tct cgt aaa gat gca atg gaa gat cag caa tat gta gta 480 Phe Ala Leu Ser Arg Lys Asp Ala Met Glu Asp Gln Gln Tyr Val Val 145 150 155 160 ctt aaa aat gac ggc ata act ttt atg tca ttg atg gtt aat act tgc 528 Leu Lys Asn Asp Gly Ile Thr Phe Met Ser Leu Met Val Asn Thr Cys 165 170 175 tat gac att aca gct gaa gga gta tct ttc gta cca tat gca tgt gca 576 Tyr Asp Ile Thr Ala Glu Gly Val Ser Phe Val Pro Tyr Ala Cys Ala 180 185 190 ggt ata gga gca gat ctt atc act att ttt aaa gac ctc aat cta aaa 624 Gly Ile Gly Ala Asp Leu Ile Thr Ile Phe Lys Asp Leu Asn Leu Lys 195 200 205 ttt gct tac caa gga aaa ata ggt att agt tac cct atc aca cca gaa 672 Phe Ala Tyr Gln Gly Lys Ile Gly Ile Ser Tyr Pro Ile Thr Pro Glu 210 215 220 gtc tct gca ttt att ggt gga tac tac cat ggc gtt att ggt aat aaa 720 Val Ser Ala Phe Ile Gly Gly Tyr Tyr His Gly Val Ile Gly Asn Lys 225 230 235 240 ttt gag aag ata cct gta ata act cct gta gta tta aat gat gct cct 768 Phe Glu Lys Ile Pro Val Ile Thr Pro Val Val Leu Asn Asp Ala Pro 245 250 255 caa acc aca tct gct tca gta act ctt gac gtt gga tac ttt ggc gga 816 Gln Thr Thr Ser Ala Ser Val Thr Leu Asp Val Gly Tyr Phe Gly Gly 260 265 270 gaa att gga atg agg ttc acc ttc taa 843 Glu Ile Gly Met Arg Phe Thr Phe 275 280 48 280 PRT Ehrlichia canis 48 Met Asn Tyr Lys Lys Ile Leu Val Arg Ser Ala Leu Ile Ser Leu Met 1 5 10 15 Ser Ile Leu Pro Tyr Gln Ser Phe Ala Asp Pro Val Gly Ser Arg Thr 20 25 30 Asn Asp Asn Lys Glu Gly Phe Tyr Ile Ser Ala Lys Tyr Asn Pro Ser 35 40 45 Ile Ser His Phe Arg Lys Phe Ser Ala Glu Glu Thr Pro Ile Asn Gly 50 55 60 Thr Asn Ser Leu Thr Lys Lys Val Phe Gly Leu Lys Lys Asp Gly Asp 65 70 75 80 Ile Thr Lys Lys Asp Asp Phe Thr Arg Val Ala Pro Gly Ile Asp Phe 85 90 95 Gln Asn Asn Leu Ile Ser Gly Phe Ser Gly Ser Ile Gly Tyr Ser Met 100 105 110 Asp Gly Pro Arg Ile Glu Leu Glu Ala Ala Tyr Gln Gln Phe Asn Pro 115 120 125 Lys Asn Thr Asp Asn Asn Asp Thr Asp Asn Gly Glu Tyr Tyr Lys His 130 135 140 Phe Ala Leu Ser Arg Lys Asp Ala Met Glu Asp Gln Gln Tyr Val Val 145 150 155 160 Leu Lys Asn Asp Gly Ile Thr Phe Met Ser Leu Met Val Asn Thr Cys 165 170 175 Tyr Asp Ile Thr Ala Glu Gly Val Ser Phe Val Pro Tyr Ala Cys Ala 180 185 190 Gly Ile Gly Ala Asp Leu Ile Thr Ile Phe Lys Asp Leu Asn Leu Lys 195 200 205 Phe Ala Tyr Gln Gly Lys Ile Gly Ile Ser Tyr Pro Ile Thr Pro Glu 210 215 220 Val Ser Ala Phe Ile Gly Gly Tyr Tyr His Gly Val Ile Gly Asn Lys 225 230 235 240 Phe Glu Lys Ile Pro Val Ile Thr Pro Val Val Leu Asn Asp Ala Pro 245 250 255 Gln Thr Thr Ser Ala Ser Val Thr Leu Asp Val Gly Tyr Phe Gly Gly 260 265 270 Glu Ile Gly Met Arg Phe Thr Phe 275 280 49 903 DNA OMP-1Z CDS (1)..(903) 49 atg aag aag aaa aat caa ttt atc aca ata agt aca ata tta gta tgt 48 Met Lys Lys Lys Asn Gln Phe Ile Thr Ile Ser Thr Ile Leu Val Cys 1 5 10 15 tta ttg tca tta tct aat gca tca ctt tca aac act aca aat agc agc 96 Leu Leu Ser Leu Ser Asn Ala Ser Leu Ser Asn Thr Thr Asn Ser Ser 20 25 30 act aaa aaa cag ttt ggg tta tat gtt agt gga caa tac aag cct agt 144 Thr Lys Lys Gln Phe Gly Leu Tyr Val Ser Gly Gln Tyr Lys Pro Ser 35 40 45 gtt tct att ttt agc aat ttc tca gta aag gaa act aat ttt cct aca 192 Val Ser Ile Phe Ser Asn Phe Ser Val Lys Glu Thr Asn Phe Pro Thr 50 55 60 aag tat cta gca gct ctt aaa aaa gac att aat tct gtc gaa ttt gac 240 Lys Tyr Leu Ala Ala Leu Lys Lys Asp Ile Asn Ser Val Glu Phe Asp 65 70 75 80 gat agt gtt act gct ggc att agt tac cca ctt aat ttc agt act cct 288 Asp Ser Val Thr Ala Gly Ile Ser Tyr Pro Leu Asn Phe Ser Thr Pro 85 90 95 tat ata gct gta ttt caa gat aat att tct aat ttt aat ggc gct att 336 Tyr Ile Ala Val Phe Gln Asp Asn Ile Ser Asn Phe Asn Gly Ala Ile 100 105 110 ggg tac act ttt gtt gaa ggc cca aga att gaa ata gaa ggt tct tat 384 Gly Tyr Thr Phe Val Glu Gly Pro Arg Ile Glu Ile Glu Gly Ser Tyr 115 120 125 gaa gaa ttc gat gtc aaa gac ctg gaa gat ata cag aaa tac aag atg 432 Glu Glu Phe Asp Val Lys Asp Leu Glu Asp Ile Gln Lys Tyr Lys Met 130 135 140 cat acc gtt gac ttt gct tta gca cgt gat ata gac tct att cct act 480 His Thr Val Asp Phe Ala Leu Ala Arg Asp Ile Asp Ser Ile Pro Thr 145 150 155 160 agc cca aaa aat aga act tca cat gat ggc aac agt tca tat aag gta 528 Ser Pro Lys Asn Arg Thr Ser His Asp Gly Asn Ser Ser Tyr Lys Val 165 170 175 tac cac act gta atg aaa aat gaa gga cta tct ata ata tcc att atg 576 Tyr His Thr Val Met Lys Asn Glu Gly Leu Ser Ile Ile Ser Ile Met 180 185 190 gtc aat ggc tgc tat gat ttt tct tca gat aat tta tca ata tta cct 624 Val Asn Gly Cys Tyr Asp Phe Ser Ser Asp Asn Leu Ser Ile Leu Pro 195 200 205 tat gta tgt ggt ggt ata ggt gta aat gct ata gag ttt ttc gat gca 672 Tyr Val Cys Gly Gly Ile Gly Val Asn Ala Ile Glu Phe Phe Asp Ala 210 215 220 tta cat gtt aaa ttc gcg tgt cag ggt aaa tta ggt att act tat cca 720 Leu His Val Lys Phe Ala Cys Gln Gly Lys Leu Gly Ile Thr Tyr Pro 225 230 235 240 tta tct tcc aac gtt agt tta ttt gct ggt gga tat tat cac caa gta 768 Leu Ser Ser Asn Val Ser Leu Phe Ala Gly Gly Tyr Tyr His Gln Val 245 250 255 atg ggc aac caa ttt aaa aat cta aat gtt caa cat gta gct gaa ctt 816 Met Gly Asn Gln Phe Lys Asn Leu Asn Val Gln His Val Ala Glu Leu 260 265 270 aat gac gca ccc aaa gtt aca tct gca gta gct aca ctt gac att ggg 864 Asn Asp Ala Pro Lys Val Thr Ser Ala Val Ala Thr Leu Asp Ile Gly 275 280 285 tat ttt ggt ggt gaa att gga gca agg ctt ata ttt taa 903 Tyr Phe Gly Gly Glu Ile Gly Ala Arg Leu Ile Phe 290 295 300 50 300 PRT OMP-1Z 50 Met Lys Lys Lys Asn Gln Phe Ile Thr Ile Ser Thr Ile Leu Val Cys 1 5 10 15 Leu Leu Ser Leu Ser Asn Ala Ser Leu Ser Asn Thr Thr Asn Ser Ser 20 25 30 Thr Lys Lys Gln Phe Gly Leu Tyr Val Ser Gly Gln Tyr Lys Pro Ser 35 40 45 Val Ser Ile Phe Ser Asn Phe Ser Val Lys Glu Thr Asn Phe Pro Thr 50 55 60 Lys Tyr Leu Ala Ala Leu Lys Lys Asp Ile Asn Ser Val Glu Phe Asp 65 70 75 80 Asp Ser Val Thr Ala Gly Ile Ser Tyr Pro Leu Asn Phe Ser Thr Pro 85 90 95 Tyr Ile Ala Val Phe Gln Asp Asn Ile Ser Asn Phe Asn Gly Ala Ile 100 105 110 Gly Tyr Thr Phe Val Glu Gly Pro Arg Ile Glu Ile Glu Gly Ser Tyr 115 120 125 Glu Glu Phe Asp Val Lys Asp Leu Glu Asp Ile Gln Lys Tyr Lys Met 130 135 140 His Thr Val Asp Phe Ala Leu Ala Arg Asp Ile Asp Ser Ile Pro Thr 145 150 155 160 Ser Pro Lys Asn Arg Thr Ser His Asp Gly Asn Ser Ser Tyr Lys Val 165 170 175 Tyr His Thr Val Met Lys Asn Glu Gly Leu Ser Ile Ile Ser Ile Met 180 185 190 Val Asn Gly Cys Tyr Asp Phe Ser Ser Asp Asn Leu Ser Ile Leu Pro 195 200 205 Tyr Val Cys Gly Gly Ile Gly Val Asn Ala Ile Glu Phe Phe Asp Ala 210 215 220 Leu His Val Lys Phe Ala Cys Gln Gly Lys Leu Gly Ile Thr Tyr Pro 225 230 235 240 Leu Ser Ser Asn Val Ser Leu Phe Ala Gly Gly Tyr Tyr His Gln Val 245 250 255 Met Gly Asn Gln Phe Lys Asn Leu Asn Val Gln His Val Ala Glu Leu 260 265 270 Asn Asp Ala Pro Lys Val Thr Ser Ala Val Ala Thr Leu Asp Ile Gly 275 280 285 Tyr Phe Gly Gly Glu Ile Gly Ala Arg Leu Ile Phe 290 295 300 51 897 DNA OMP-1H CDS (1)..(897) 51 atg aat cac aaa agt atg ctc ttt aca ata ggt aca gct ttg ata tcc 48 Met Asn His Lys Ser Met Leu Phe Thr Ile Gly Thr Ala Leu Ile Ser 1 5 10 15 tta ttg tca tta cct aat gta tca ttc tca gga atc ata aat aac aat 96 Leu Leu Ser Leu Pro Asn Val Ser Phe Ser Gly Ile Ile Asn Asn Asn 20 25 30 gct aac aat tta ggt ata tac att agt ggg caa tat aaa ccc agt gtt 144 Ala Asn Asn Leu Gly Ile Tyr Ile Ser Gly Gln Tyr Lys Pro Ser Val 35 40 45 tct gtt ttt agc aat ttc tca gta aaa gaa act aac ttc act aca caa 192 Ser Val Phe Ser Asn Phe Ser Val Lys Glu Thr Asn Phe Thr Thr Gln 50 55 60 cag tta gta gca ctt aaa aaa gat att gat tct gtt gac att agt acc 240 Gln Leu Val Ala Leu Lys Lys Asp Ile Asp Ser Val Asp Ile Ser Thr 65 70 75 80 aat gct gat agc ggt att aat aat ccg cag aat ttc act atc cct tat 288 Asn Ala Asp Ser Gly Ile Asn Asn Pro Gln Asn Phe Thr Ile Pro Tyr 85 90 95 ata cca aaa ttt caa gac aat gct gct agt ttt agt gga gca ctt gga 336 Ile Pro Lys Phe Gln Asp Asn Ala Ala Ser Phe Ser Gly Ala Leu Gly 100 105 110 ttc ttc tac gct aga ggt tta aga ctt gaa atg gaa ggt tcc tat gaa 384 Phe Phe Tyr Ala Arg Gly Leu Arg Leu Glu Met Glu Gly Ser Tyr Glu 115 120 125 gaa ttt gat gtt aaa aac cct gga gga tat aca aaa gta aaa gat gca 432 Glu Phe Asp Val Lys Asn Pro Gly Gly Tyr Thr Lys Val Lys Asp Ala 130 135 140 tat cgt tac ttt gcc ctg gca cgt gag atg caa tct ggt caa act tgc 480 Tyr Arg Tyr Phe Ala Leu Ala Arg Glu Met Gln Ser Gly Gln Thr Cys 145 150 155 160 cct aaa cac aaa gaa aca tca ggt att caa cct cac ggt att tat cac 528 Pro Lys His Lys Glu Thr Ser Gly Ile Gln Pro His Gly Ile Tyr His 165 170 175 act gtt atg agg aat gat ggg gta tct att tca tct gtc ata atc aat 576 Thr Val Met Arg Asn Asp Gly Val Ser Ile Ser Ser Val Ile Ile Asn 180 185 190 ggt tgt tat aac ttt act tta agt aat cta cca ata tca cct tac atg 624 Gly Cys Tyr Asn Phe Thr Leu Ser Asn Leu Pro Ile Ser Pro Tyr Met 195 200 205 tgt gta ggt atg gga ata gat gct ata caa ttt ttt gat tca cta cat 672 Cys Val Gly Met Gly Ile Asp Ala Ile Gln Phe Phe Asp Ser Leu His 210 215 220 att aag ttt gca cat caa agt aag tta ggt att act tac cca cta tct 720 Ile Lys Phe Ala His Gln Ser Lys Leu Gly Ile Thr Tyr Pro Leu Ser 225 230 235 240 tca aat gtt cat tta ttt gct gat agc tat tat cat aaa gta ata ggt 768 Ser Asn Val His Leu Phe Ala Asp Ser Tyr Tyr His Lys Val Ile Gly 245 250 255 aat aaa ttt aaa aat cta agg gtt caa cac gtt tat gaa tta caa cag 816 Asn Lys Phe Lys Asn Leu Arg Val Gln His Val Tyr Glu Leu Gln Gln 260 265 270 gta cct aaa gtt aca tct gct gtt gct aca ctt gat att ggg tat ttt 864 Val Pro Lys Val Thr Ser Ala Val Ala Thr Leu Asp Ile Gly Tyr Phe 275 280 285 ggt ggt gaa gtt gga gta agg ttt ata ctt taa 897 Gly Gly Glu Val Gly Val Arg Phe Ile Leu 290 295 52 298 PRT OMP-1H 52 Met Asn His Lys Ser Met Leu Phe Thr Ile Gly Thr Ala Leu Ile Ser 1 5 10 15 Leu Leu Ser Leu Pro Asn Val Ser Phe Ser Gly Ile Ile Asn Asn Asn 20 25 30 Ala Asn Asn Leu Gly Ile Tyr Ile Ser Gly Gln Tyr Lys Pro Ser Val 35 40 45 Ser Val Phe Ser Asn Phe Ser Val Lys Glu Thr Asn Phe Thr Thr Gln 50 55 60 Gln Leu Val Ala Leu Lys Lys Asp Ile Asp Ser Val Asp Ile Ser Thr 65 70 75 80 Asn Ala Asp Ser Gly Ile Asn Asn Pro Gln Asn Phe Thr Ile Pro Tyr 85 90 95 Ile Pro Lys Phe Gln Asp Asn Ala Ala Ser Phe Ser Gly Ala Leu Gly 100 105 110 Phe Phe Tyr Ala Arg Gly Leu Arg Leu Glu Met Glu Gly Ser Tyr Glu 115 120 125 Glu Phe Asp Val Lys Asn Pro Gly Gly Tyr Thr Lys Val Lys Asp Ala 130 135 140 Tyr Arg Tyr Phe Ala Leu Ala Arg Glu Met Gln Ser Gly Gln Thr Cys 145 150 155 160 Pro Lys His Lys Glu Thr Ser Gly Ile Gln Pro His Gly Ile Tyr His 165 170 175 Thr Val Met Arg Asn Asp Gly Val Ser Ile Ser Ser Val Ile Ile Asn 180 185 190 Gly Cys Tyr Asn Phe Thr Leu Ser Asn Leu Pro Ile Ser Pro Tyr Met 195 200 205 Cys Val Gly Met Gly Ile Asp Ala Ile Gln Phe Phe Asp Ser Leu His 210 215 220 Ile Lys Phe Ala His Gln Ser Lys Leu Gly Ile Thr Tyr Pro Leu Ser 225 230 235 240 Ser Asn Val His Leu Phe Ala Asp Ser Tyr Tyr His Lys Val Ile Gly 245 250 255 Asn Lys Phe Lys Asn Leu Arg Val Gln His Val Tyr Glu Leu Gln Gln 260 265 270 Val Pro Lys Val Thr Ser Ala Val Ala Thr Leu Asp Ile Gly Tyr Phe 275 280 285 Gly Gly Glu Val Gly Val Arg Phe Ile Leu 290 295 53 882 DNA p30-6 CDS (1)..(882) 53 atg gca aat ttt atg tac aaa aaa tac aaa cta atg aca gca ggt gta 48 Met Ala Asn Phe Met Tyr Lys Lys Tyr Lys Leu Met Thr Ala Gly Val 1 5 10 15 gta tta ttt cac atg tta ttt cta cct cat gtt tct ttc gca aaa aat 96 Val Leu Phe His Met Leu Phe Leu Pro His Val Ser Phe Ala Lys Asn 20 25 30 aca aac agc aat aaa ctt gga tta tac atc agt gga cag tat aac cct 144 Thr Asn Ser Asn Lys Leu Gly Leu Tyr Ile Ser Gly Gln Tyr Asn Pro 35 40 45 agt gtt tct gtt ttt agc aat ttt tca gca aaa gaa acc aat gtt cat 192 Ser Val Ser Val Phe Ser Asn Phe Ser Ala Lys Glu Thr Asn Val His 50 55 60 aca gta caa ctc atg gcg ctt aaa aaa gac att gat tct att gaa gtt 240 Thr Val Gln Leu Met Ala Leu Lys Lys Asp Ile Asp Ser Ile Glu Val 65 70 75 80 gat act gga aat agc gca ggt att agc aaa cca caa aat ttc aca gtt 288 Asp Thr Gly Asn Ser Ala Gly Ile Ser Lys Pro Gln Asn Phe Thr Val 85 90 95 ctt tat act cca aaa ttt caa gat aat gtt gct ggt ctt agc ggt gca 336 Leu Tyr Thr Pro Lys Phe Gln Asp Asn Val Ala Gly Leu Ser Gly Ala 100 105 110 ctt gga ttc ttt tat tct aaa gga tta agg att gaa atg ggg ttt tct 384 Leu Gly Phe Phe Tyr Ser Lys Gly Leu Arg Ile Glu Met Gly Phe Ser 115 120 125 tat gaa aaa ttt gat gct aaa gac ctt ggt gag tac acc aaa ata aaa 432 Tyr Glu Lys Phe Asp Ala Lys Asp Leu Gly Glu Tyr Thr Lys Ile Lys 130 135 140 gat gct tat aga tat ttt gct cta gta cgt gaa atg cat gtt agt ctc 480 Asp Ala Tyr Arg Tyr Phe Ala Leu Val Arg Glu Met His Val Ser Leu 145 150 155 160 att tat cca aaa gat aat aac aca gga aca cat tat act gtt atg aga 528 Ile Tyr Pro Lys Asp Asn Asn Thr Gly Thr His Tyr Thr Val Met Arg 165 170 175 aat gat ggt ata tct att tct tct gct aca gta aat ggc tgc tat gat 576 Asn Asp Gly Ile Ser Ile Ser Ser Ala Thr Val Asn Gly Cys Tyr Asp 180 185 190 tct ttt ttc cag ttt atc ttt gtc acc tat atg tgt ata ggc atc ggt 624 Ser Phe Phe Gln Phe Ile Phe Val Thr Tyr Met Cys Ile Gly Ile Gly 195 200 205 ata gat gct ata gaa ttt ctt aat gca tac ata tta agt ttg ctt gcc 672 Ile Asp Ala Ile Glu Phe Leu Asn Ala Tyr Ile Leu Ser Leu Leu Ala 210 215 220 aag gta gtt aag gtg tta act tat tct gta tct ccc aat gtt aat tta 720 Lys Val Val Lys Val Leu Thr Tyr Ser Val Ser Pro Asn Val Asn Leu 225 230 235 240 ttt gca gat gga tat tat cat aaa gtg atg ggc aat aaa ttt aaa aat 768 Phe Ala Asp Gly Tyr Tyr His Lys Val Met Gly Asn Lys Phe Lys Asn 245 250 255 tta cct gtt caa tac gtt aat act tta gaa gag tat cca aga gtt aca 816 Leu Pro Val Gln Tyr Val Asn Thr Leu Glu Glu Tyr Pro Arg Val Thr 260 265 270 tct gca att gct aca ctt gat att ggc tac ctc ggt ggt gaa att ggc 864 Ser Ala Ile Ala Thr Leu Asp Ile Gly Tyr Leu Gly Gly Glu Ile Gly 275 280 285 ata aga ttt ata ttt taa 882 Ile Arg Phe Ile Phe 290 54 293 PRT p30-6 54 Met Ala Asn Phe Met Tyr Lys Lys Tyr Lys Leu Met Thr Ala Gly Val 1 5 10 15 Val Leu Phe His Met Leu Phe Leu Pro His Val Ser Phe Ala Lys Asn 20 25 30 Thr Asn Ser Asn Lys Leu Gly Leu Tyr Ile Ser Gly Gln Tyr Asn Pro 35 40 45 Ser Val Ser Val Phe Ser Asn Phe Ser Ala Lys Glu Thr Asn Val His 50 55 60 Thr Val Gln Leu Met Ala Leu Lys Lys Asp Ile Asp Ser Ile Glu Val 65 70 75 80 Asp Thr Gly Asn Ser Ala Gly Ile Ser Lys Pro Gln Asn Phe Thr Val 85 90 95 Leu Tyr Thr Pro Lys Phe Gln Asp Asn Val Ala Gly Leu Ser Gly Ala 100 105 110 Leu Gly Phe Phe Tyr Ser Lys Gly Leu Arg Ile Glu Met Gly Phe Ser 115 120 125 Tyr Glu Lys Phe Asp Ala Lys Asp Leu Gly Glu Tyr Thr Lys Ile Lys 130 135 140 Asp Ala Tyr Arg Tyr Phe Ala Leu Val Arg Glu Met His Val Ser Leu 145 150 155 160 Ile Tyr Pro Lys Asp Asn Asn Thr Gly Thr His Tyr Thr Val Met Arg 165 170 175 Asn Asp Gly Ile Ser Ile Ser Ser Ala Thr Val Asn Gly Cys Tyr Asp 180 185 190 Ser Phe Phe Gln Phe Ile Phe Val Thr Tyr Met Cys Ile Gly Ile Gly 195 200 205 Ile Asp Ala Ile Glu Phe Leu Asn Ala Tyr Ile Leu Ser Leu Leu Ala 210 215 220 Lys Val Val Lys Val Leu Thr Tyr Ser Val Ser Pro Asn Val Asn Leu 225 230 235 240 Phe Ala Asp Gly Tyr Tyr His Lys Val Met Gly Asn Lys Phe Lys Asn 245 250 255 Leu Pro Val Gln Tyr Val Asn Thr Leu Glu Glu Tyr Pro Arg Val Thr 260 265 270 Ser Ala Ile Ala Thr Leu Asp Ile Gly Tyr Leu Gly Gly Glu Ile Gly 275 280 285 Ile Arg Phe Ile Phe 290 55 891 DNA p30-7 CDS (1)..(891) 55 atg gga aat tct atg aat aat aaa agt caa ttc tta ata aga ttt ata 48 Met Gly Asn Ser Met Asn Asn Lys Ser Gln Phe Leu Ile Arg Phe Ile 1 5 10 15 ttt tta aca tgc atg ctg tca tta cct aat ata tct ctt tca aaa gta 96 Phe Leu Thr Cys Met Leu Ser Leu Pro Asn Ile Ser Leu Ser Lys Val 20 25 30 aat aac gaa aaa cat tct ggt ttg tat att agc ggg caa tac aaa ccc 144 Asn Asn Glu Lys His Ser Gly Leu Tyr Ile Ser Gly Gln Tyr Lys Pro 35 40 45 agt gtt tct gtt ttc agt aat ttt tca gtt aaa gaa acc aac ttt cat 192 Ser Val Ser Val Phe Ser Asn Phe Ser Val Lys Glu Thr Asn Phe His 50 55 60 aca aaa cat ctc ata gct ctt aaa caa gat gtt gat tct gtt gaa att 240 Thr Lys His Leu Ile Ala Leu Lys Gln Asp Val Asp Ser Val Glu Ile 65 70 75 80 gat act ggt agt aat aca gca ggt att agt aac cca tct aac ttt aca 288 Asp Thr Gly Ser Asn Thr Ala Gly Ile Ser Asn Pro Ser Asn Phe Thr 85 90 95 atc cct tat act gca gaa ttt caa gac aac cat act aac tgc aat ggc 336 Ile Pro Tyr Thr Ala Glu Phe Gln Asp Asn His Thr Asn Cys Asn Gly 100 105 110 tct att ggt tat gct ttt gct gaa ggt cca aga att gaa ata gaa tta 384 Ser Ile Gly Tyr Ala Phe Ala Glu Gly Pro Arg Ile Glu Ile Glu Leu 115 120 125 tca tat gaa aaa ttt gat gtt aaa aat ccc aca ggg tat act aca gta 432 Ser Tyr Glu Lys Phe Asp Val Lys Asn Pro Thr Gly Tyr Thr Thr Val 130 135 140 aaa gat gct tat aga tac ttt gct tta gca cgt gaa ata aat att tct 480 Lys Asp Ala Tyr Arg Tyr Phe Ala Leu Ala Arg Glu Ile Asn Ile Ser 145 150 155 160 cta ttc caa cca aaa caa aaa gaa ggt agt gga att tac cat gtc gta 528 Leu Phe Gln Pro Lys Gln Lys Glu Gly Ser Gly Ile Tyr His Val Val 165 170 175 atg aaa aac gat ggg tta tct atc tta tcc aat ata gtt aat att tgc 576 Met Lys Asn Asp Gly Leu Ser Ile Leu Ser Asn Ile Val Asn Ile Cys 180 185 190 tac gat ttt tct tta aat aat tta cct ata tca cct tat tta tgc gga 624 Tyr Asp Phe Ser Leu Asn Asn Leu Pro Ile Ser Pro Tyr Leu Cys Gly 195 200 205 gga atg ggt ata aat gcc ata gaa ttc ttt gac gct tta cat gtg aaa 672 Gly Met Gly Ile Asn Ala Ile Glu Phe Phe Asp Ala Leu His Val Lys 210 215 220 ttt gct tat caa agc aag gca gga att agt tat caa cta tta cgt aaa 720 Phe Ala Tyr Gln Ser Lys Ala Gly Ile Ser Tyr Gln Leu Leu Arg Lys 225 230 235 240 atc aac tta ttt att gat gta tat tac tac gaa gta ata agt aat aaa 768 Ile Asn Leu Phe Ile Asp Val Tyr Tyr Tyr Glu Val Ile Ser Asn Lys 245 250 255 ttt aaa aac ctg aaa gtc caa cat gta cat gaa ctt aaa gat aat cca 816 Phe Lys Asn Leu Lys Val Gln His Val His Glu Leu Lys Asp Asn Pro 260 265 270 aaa gtc aca tct gca gtt gct aca ctt gat ata gca tat ttt ggt agt 864 Lys Val Thr Ser Ala Val Ala Thr Leu Asp Ile Ala Tyr Phe Gly Ser 275 280 285 gaa gct ggc ata aga att ata ttt taa 891 Glu Ala Gly Ile Arg Ile Ile Phe 290 295 56 296 PRT p30-7 56 Met Gly Asn Ser Met Asn Asn Lys Ser Gln Phe Leu Ile Arg Phe Ile 1 5 10 15 Phe Leu Thr Cys Met Leu Ser Leu Pro Asn Ile Ser Leu Ser Lys Val 20 25 30 Asn Asn Glu Lys His Ser Gly Leu Tyr Ile Ser Gly Gln Tyr Lys Pro 35 40 45 Ser Val Ser Val Phe Ser Asn Phe Ser Val Lys Glu Thr Asn Phe His 50 55 60 Thr Lys His Leu Ile Ala Leu Lys Gln Asp Val Asp Ser Val Glu Ile 65 70 75 80 Asp Thr Gly Ser Asn Thr Ala Gly Ile Ser Asn Pro Ser Asn Phe Thr 85 90 95 Ile Pro Tyr Thr Ala Glu Phe Gln Asp Asn His Thr Asn Cys Asn Gly 100 105 110 Ser Ile Gly Tyr Ala Phe Ala Glu Gly Pro Arg Ile Glu Ile Glu Leu 115 120 125 Ser Tyr Glu Lys Phe Asp Val Lys Asn Pro Thr Gly Tyr Thr Thr Val 130 135 140 Lys Asp Ala Tyr Arg Tyr Phe Ala Leu Ala Arg Glu Ile Asn Ile Ser 145 150 155 160 Leu Phe Gln Pro Lys Gln Lys Glu Gly Ser Gly Ile Tyr His Val Val 165 170 175 Met Lys Asn Asp Gly Leu Ser Ile Leu Ser Asn Ile Val Asn Ile Cys 180 185 190 Tyr Asp Phe Ser Leu Asn Asn Leu Pro Ile Ser Pro Tyr Leu Cys Gly 195 200 205 Gly Met Gly Ile Asn Ala Ile Glu Phe Phe Asp Ala Leu His Val Lys 210 215 220 Phe Ala Tyr Gln Ser Lys Ala Gly Ile Ser Tyr Gln Leu Leu Arg Lys 225 230 235 240 Ile Asn Leu Phe Ile Asp Val Tyr Tyr Tyr Glu Val Ile Ser Asn Lys 245 250 255 Phe Lys Asn Leu Lys Val Gln His Val His Glu Leu Lys Asp Asn Pro 260 265 270 Lys Val Thr Ser Ala Val Ala Thr Leu Asp Ile Ala Tyr Phe Gly Ser 275 280 285 Glu Ala Gly Ile Arg Ile Ile Phe 290 295 57 846 DNA p30-9 CDS (1)..(846) 57 atg aat aat aaa aga aat ttt ttt tta ata ggt atg tct cta ttg ata 48 Met Asn Asn Lys Arg Asn Phe Phe Leu Ile Gly Met Ser Leu Leu Ile 1 5 10 15 aat cta cta ttg cca att gat gcc tct tct atg gaa gta cat aat tat 96 Asn Leu Leu Leu Pro Ile Asp Ala Ser Ser Met Glu Val His Asn Tyr 20 25 30 aca cat ttt aca cct agg ctg tat att agt ggg caa tac agg cca gga 144 Thr His Phe Thr Pro Arg Leu Tyr Ile Ser Gly Gln Tyr Arg Pro Gly 35 40 45 gtt tcc cac ttt agc aaa ttt tca gtc aaa gaa aca cat tgt aat act 192 Val Ser His Phe Ser Lys Phe Ser Val Lys Glu Thr His Cys Asn Thr 50 55 60 gtg caa tta gtt ggg cta aca aaa gat ata aaa gta act aat aac agt 240 Val Gln Leu Val Gly Leu Thr Lys Asp Ile Lys Val Thr Asn Asn Ser 65 70 75 80 agt atc aac aca aat act agt ttt aac ttt cct tat gtt gca gaa ttt 288 Ser Ile Asn Thr Asn Thr Ser Phe Asn Phe Pro Tyr Val Ala Glu Phe 85 90 95 caa gat aac gca atg agc ttt agt gga gca ata gga tgc ttt tat tca 336 Gln Asp Asn Ala Met Ser Phe Ser Gly Ala Ile Gly Cys Phe Tyr Ser 100 105 110 gaa cac ttc aga att gaa gta gaa gct tct tat gaa gaa ttt gac gtt 384 Glu His Phe Arg Ile Glu Val Glu Ala Ser Tyr Glu Glu Phe Asp Val 115 120 125 aaa aat cct gaa gga tct act aca gac tcc tat aga tat ttc gcg tta 432 Lys Asn Pro Glu Gly Ser Thr Thr Asp Ser Tyr Arg Tyr Phe Ala Leu 130 135 140 gca cgt ggc atg gat ggt aat aat att cct aca agt caa aaa ttt act 480 Ala Arg Gly Met Asp Gly Asn Asn Ile Pro Thr Ser Gln Lys Phe Thr 145 150 155 160 gta atg aga aac gac ggg tta tta atc tca tct gtt atg ata aat ggc 528 Val Met Arg Asn Asp Gly Leu Leu Ile Ser Ser Val Met Ile Asn Gly 165 170 175 tgt tac aat gtc ata cta aat gat ata caa gca gaa cct tac ata tgt 576 Cys Tyr Asn Val Ile Leu Asn Asp Ile Gln Ala Glu Pro Tyr Ile Cys 180 185 190 gca gga cta gga gga gat ttt ata gaa ttc ttc aat ggc ttt cat gtt 624 Ala Gly Leu Gly Gly Asp Phe Ile Glu Phe Phe Asn Gly Phe His Val 195 200 205 aag cta gct tat caa ggt aaa gta ggc att agt tat caa ata ttc cct 672 Lys Leu Ala Tyr Gln Gly Lys Val Gly Ile Ser Tyr Gln Ile Phe Pro 210 215 220 gaa gta aga tta ttt att gat gga tac tac cat aaa gta aaa ggc aac 720 Glu Val Arg Leu Phe Ile Asp Gly Tyr Tyr His Lys Val Lys Gly Asn 225 230 235 240 aag ttt aaa aat tta cac gtt caa cat gta ggt gca ctt gca gca ctc 768 Lys Phe Lys Asn Leu His Val Gln His Val Gly Ala Leu Ala Ala Leu 245 250 255 cct aaa gtt aca tct gca gtt gca aca ctt aat att gga tac ttt ggt 816 Pro Lys Val Thr Ser Ala Val Ala Thr Leu Asn Ile Gly Tyr Phe Gly 260 265 270 tgt gaa gct gga gta aga ttc ata ttt taa 846 Cys Glu Ala Gly Val Arg Phe Ile Phe 275 280 58 281 PRT p30-9 58 Met Asn Asn Lys Arg Asn Phe Phe Leu Ile Gly Met Ser Leu Leu Ile 1 5 10 15 Asn Leu Leu Leu Pro Ile Asp Ala Ser Ser Met Glu Val His Asn Tyr 20 25 30 Thr His Phe Thr Pro Arg Leu Tyr Ile Ser Gly Gln Tyr Arg Pro Gly 35 40 45 Val Ser His Phe Ser Lys Phe Ser Val Lys Glu Thr His Cys Asn Thr 50 55 60 Val Gln Leu Val Gly Leu Thr Lys Asp Ile Lys Val Thr Asn Asn Ser 65 70 75 80 Ser Ile Asn Thr Asn Thr Ser Phe Asn Phe Pro Tyr Val Ala Glu Phe 85 90 95 Gln Asp Asn Ala Met Ser Phe Ser Gly Ala Ile Gly Cys Phe Tyr Ser 100 105 110 Glu His Phe Arg Ile Glu Val Glu Ala Ser Tyr Glu Glu Phe Asp Val 115 120 125 Lys Asn Pro Glu Gly Ser Thr Thr Asp Ser Tyr Arg Tyr Phe Ala Leu 130 135 140 Ala Arg Gly Met Asp Gly Asn Asn Ile Pro Thr Ser Gln Lys Phe Thr 145 150 155 160 Val Met Arg Asn Asp Gly Leu Leu Ile Ser Ser Val Met Ile Asn Gly 165 170 175 Cys Tyr Asn Val Ile Leu Asn Asp Ile Gln Ala Glu Pro Tyr Ile Cys 180 185 190 Ala Gly Leu Gly Gly Asp Phe Ile Glu Phe Phe Asn Gly Phe His Val 195 200 205 Lys Leu Ala Tyr Gln Gly Lys Val Gly Ile Ser Tyr Gln Ile Phe Pro 210 215 220 Glu Val Arg Leu Phe Ile Asp Gly Tyr Tyr His Lys Val Lys Gly Asn 225 230 235 240 Lys Phe Lys Asn Leu His Val Gln His Val Gly Ala Leu Ala Ala Leu 245 250 255 Pro Lys Val Thr Ser Ala Val Ala Thr Leu Asn Ile Gly Tyr Phe Gly 260 265 270 Cys Glu Ala Gly Val Arg Phe Ile Phe 275 280 59 840 DNA p30-11 CDS (1)..(840) 59 atg aac aaa aag aaa att att aca gta gga aca aca tta gct tat tta 48 Met Asn Lys Lys Lys Ile Ile Thr Val Gly Thr Thr Leu Ala Tyr Leu 1 5 10 15 tta tta tca cct aac ata tct ttt tca gaa gta atc aac aat gat act 96 Leu Leu Ser Pro Asn Ile Ser Phe Ser Glu Val Ile Asn Asn Asp Thr 20 25 30 gat aaa tat tct aga cta tat ata agt ggt caa tat aaa cca gga ttt 144 Asp Lys Tyr Ser Arg Leu Tyr Ile Ser Gly Gln Tyr Lys Pro Gly Phe 35 40 45 tct tat ttt aat aag ttc tca gtt aga gaa act gat cat ttc act aaa 192 Ser Tyr Phe Asn Lys Phe Ser Val Arg Glu Thr Asp His Phe Thr Lys 50 55 60 gca tta ata gga tta aga cat gac gca ata tct act aaa aat tta aca 240 Ala Leu Ile Gly Leu Arg His Asp Ala Ile Ser Thr Lys Asn Leu Thr 65 70 75 80 act aat aca gat ttc aat act ctt tat aaa gta aca ttt caa aac aac 288 Thr Asn Thr Asp Phe Asn Thr Leu Tyr Lys Val Thr Phe Gln Asn Asn 85 90 95 atc att agc ttt agc ggt gct att ggt tat tct gat agc aca ggt gta 336 Ile Ile Ser Phe Ser Gly Ala Ile Gly Tyr Ser Asp Ser Thr Gly Val 100 105 110 agg ttt gag cta gaa ggc tct tat gaa gag ttc gat gtt aca gac cct 384 Arg Phe Glu Leu Glu Gly Ser Tyr Glu Glu Phe Asp Val Thr Asp Pro 115 120 125 gga gat tgt ata ata aaa gat act tac agg tac ttt gca tta gct aga 432 Gly Asp Cys Ile Ile Lys Asp Thr Tyr Arg Tyr Phe Ala Leu Ala Arg 130 135 140 aaa aca agt ggt aat cat ccc aac gat aat ggg gaa tat act gtc atg 480 Lys Thr Ser Gly Asn His Pro Asn Asp Asn Gly Glu Tyr Thr Val Met 145 150 155 160 aga aat gat gga gta tcc att acc tcc gtt ata ttc aat ggt tgt tat 528 Arg Asn Asp Gly Val Ser Ile Thr Ser Val Ile Phe Asn Gly Cys Tyr 165 170 175 gat ctc tct tta aaa gag cta gaa ata tca cca tat gtt tgc att ggt 576 Asp Leu Ser Leu Lys Glu Leu Glu Ile Ser Pro Tyr Val Cys Ile Gly 180 185 190 atc gga gga gac ttt ata gaa ttt ttt gat gct tta cac att aaa tta 624 Ile Gly Gly Asp Phe Ile Glu Phe Phe Asp Ala Leu His Ile Lys Leu 195 200 205 gca tat caa ggt aaa cta ggt att agc tat tct ttt tcc act aga aca 672 Ala Tyr Gln Gly Lys Leu Gly Ile Ser Tyr Ser Phe Ser Thr Arg Thr 210 215 220 aat tta ttt atc gat tgt tat tac cat aga gtt ata ggt aat caa ttt 720 Asn Leu Phe Ile Asp Cys Tyr Tyr His Arg Val Ile Gly Asn Gln Phe 225 230 235 240 aat aat tta aat gtt caa cat gta gtt gag ctt aca gaa gca cct aaa 768 Asn Asn Leu Asn Val Gln His Val Val Glu Leu Thr Glu Ala Pro Lys 245 250 255 gct aca tct gca att gct aca ctt aat gtt agt tac ttc ggt gga gaa 816 Ala Thr Ser Ala Ile Ala Thr Leu Asn Val Ser Tyr Phe Gly Gly Glu 260 265 270 gtt gga att aga ctt atg ttt taa 840 Val Gly Ile Arg Leu Met Phe 275 280 60 279 PRT p30-11 60 Met Asn Lys Lys Lys Ile Ile Thr Val Gly Thr Thr Leu Ala Tyr Leu 1 5 10 15 Leu Leu Ser Pro Asn Ile Ser Phe Ser Glu Val Ile Asn Asn Asp Thr 20 25 30 Asp Lys Tyr Ser Arg Leu Tyr Ile Ser Gly Gln Tyr Lys Pro Gly Phe 35 40 45 Ser Tyr Phe Asn Lys Phe Ser Val Arg Glu Thr Asp His Phe Thr Lys 50 55 60 Ala Leu Ile Gly Leu Arg His Asp Ala Ile Ser Thr Lys Asn Leu Thr 65 70 75 80 Thr Asn Thr Asp Phe Asn Thr Leu Tyr Lys Val Thr Phe Gln Asn Asn 85 90 95 Ile Ile Ser Phe Ser Gly Ala Ile Gly Tyr Ser Asp Ser Thr Gly Val 100 105 110 Arg Phe Glu Leu Glu Gly Ser Tyr Glu Glu Phe Asp Val Thr Asp Pro 115 120 125 Gly Asp Cys Ile Ile Lys Asp Thr Tyr Arg Tyr Phe Ala Leu Ala Arg 130 135 140 Lys Thr Ser Gly Asn His Pro Asn Asp Asn Gly Glu Tyr Thr Val Met 145 150 155 160 Arg Asn Asp Gly Val Ser Ile Thr Ser Val Ile Phe Asn Gly Cys Tyr 165 170 175 Asp Leu Ser Leu Lys Glu Leu Glu Ile Ser Pro Tyr Val Cys Ile Gly 180 185 190 Ile Gly Gly Asp Phe Ile Glu Phe Phe Asp Ala Leu His Ile Lys Leu 195 200 205 Ala Tyr Gln Gly Lys Leu Gly Ile Ser Tyr Ser Phe Ser Thr Arg Thr 210 215 220 Asn Leu Phe Ile Asp Cys Tyr Tyr His Arg Val Ile Gly Asn Gln Phe 225 230 235 240 Asn Asn Leu Asn Val Gln His Val Val Glu Leu Thr Glu Ala Pro Lys 245 250 255 Ala Thr Ser Ala Ile Ala Thr Leu Asn Val Ser Tyr Phe Gly Gly Glu 260 265 270 Val Gly Ile Arg Leu Met Phe 275 61 726 DNA p30-12 CDS (1)..(726) 61 ccc gtc gtt tct cat tac agt gac ttt tca att aaa gaa act tat act 48 Pro Val Val Ser His Tyr Ser Asp Phe Ser Ile Lys Glu Thr Tyr Thr 1 5 10 15 aac act gag gca ttg ttt ggg cta aaa caa gat att agt tct att tta 96 Asn Thr Glu Ala Leu Phe Gly Leu Lys Gln Asp Ile Ser Ser Ile Leu 20 25 30 cgt aat aaa gag acc aca caa tat aat aac aat ttt aac gtt ccc tat 144 Arg Asn Lys Glu Thr Thr Gln Tyr Asn Asn Asn Phe Asn Val Pro Tyr 35 40 45 act gca aaa ttt caa gac gac ttt gcg agt ttc agc ata gct gtt gga 192 Thr Ala Lys Phe Gln Asp Asp Phe Ala Ser Phe Ser Ile Ala Val Gly 50 55 60 tat att gct aac aat ggt cca aga att gaa ata gaa gga tct tac gaa 240 Tyr Ile Ala Asn Asn Gly Pro Arg Ile Glu Ile Glu Gly Ser Tyr Glu 65 70 75 80 gaa ttt gat gtt aaa aac cca gga aat tat aca aca ata gat gct cat 288 Glu Phe Asp Val Lys Asn Pro Gly Asn Tyr Thr Thr Ile Asp Ala His 85 90 95 agg tac att gct tta gct aga gaa aaa act tct tac tat cta agt tct 336 Arg Tyr Ile Ala Leu Ala Arg Glu Lys Thr Ser Tyr Tyr Leu Ser Ser 100 105 110 cct aaa gaa aac aaa tat gta att ata aag aat aac ggc ata tct att 384 Pro Lys Glu Asn Lys Tyr Val Ile Ile Lys Asn Asn Gly Ile Ser Ile 115 120 125 gta tct att ata att aat ggt tgt tat gat att tct tta aat gat tct 432 Val Ser Ile Ile Ile Asn Gly Cys Tyr Asp Ile Ser Leu Asn Asp Ser 130 135 140 aag gtg tca cct tac ata tgc aca ggg ttt ggt gga gat ttt ata gag 480 Lys Val Ser Pro Tyr Ile Cys Thr Gly Phe Gly Gly Asp Phe Ile Glu 145 150 155 160 ttt ttt agt gct ata cgt ttt aag ttt gct tat caa ggt aaa ata ggt 528 Phe Phe Ser Ala Ile Arg Phe Lys Phe Ala Tyr Gln Gly Lys Ile Gly 165 170 175 atc agt tat tca tta tct tct aac ata att tta ttt act gat gga tat 576 Ile Ser Tyr Ser Leu Ser Ser Asn Ile Ile Leu Phe Thr Asp Gly Tyr 180 185 190 tac cac aag gta ata aat tcc caa ttt aaa aat tta aat gtt gaa cat 624 Tyr His Lys Val Ile Asn Ser Gln Phe Lys Asn Leu Asn Val Glu His 195 200 205 gtt gtt aat gag tta act aca gat cct aaa gtg act tct gca aca gca 672 Val Val Asn Glu Leu Thr Thr Asp Pro Lys Val Thr Ser Ala Thr Ala 210 215 220 ttt ctt aat att gag tat ttt ggt ggt gaa ttt gga tta aaa ttt ata 720 Phe Leu Asn Ile Glu Tyr Phe Gly Gly Glu Phe Gly Leu Lys Phe Ile 225 230 235 240 ttt taa 726 Phe 62 241 PRT p30-12 62 Pro Val Val Ser His Tyr Ser Asp Phe Ser Ile Lys Glu Thr Tyr Thr 1 5 10 15 Asn Thr Glu Ala Leu Phe Gly Leu Lys Gln Asp Ile Ser Ser Ile Leu 20 25 30 Arg Asn Lys Glu Thr Thr Gln Tyr Asn Asn Asn Phe Asn Val Pro Tyr 35 40 45 Thr Ala Lys Phe Gln Asp Asp Phe Ala Ser Phe Ser Ile Ala Val Gly 50 55 60 Tyr Ile Ala Asn Asn Gly Pro Arg Ile Glu Ile Glu Gly Ser Tyr Glu 65 70 75 80 Glu Phe Asp Val Lys Asn Pro Gly Asn Tyr Thr Thr Ile Asp Ala His 85 90 95 Arg Tyr Ile Ala Leu Ala Arg Glu Lys Thr Ser Tyr Tyr Leu Ser Ser 100 105 110 Pro Lys Glu Asn Lys Tyr Val Ile Ile Lys Asn Asn Gly Ile Ser Ile 115 120 125 Val Ser Ile Ile Ile Asn Gly Cys Tyr Asp Ile Ser Leu Asn Asp Ser 130 135 140 Lys Val Ser Pro Tyr Ile Cys Thr Gly Phe Gly Gly Asp Phe Ile Glu 145 150 155 160 Phe Phe Ser Ala Ile Arg Phe Lys Phe Ala Tyr Gln Gly Lys Ile Gly 165 170 175 Ile Ser Tyr Ser Leu Ser Ser Asn Ile Ile Leu Phe Thr Asp Gly Tyr 180 185 190 Tyr His Lys Val Ile Asn Ser Gln Phe Lys Asn Leu Asn Val Glu His 195 200 205 Val Val Asn Glu Leu Thr Thr Asp Pro Lys Val Thr Ser Ala Thr Ala 210 215 220 Phe Leu Asn Ile Glu Tyr Phe Gly Gly Glu Phe Gly Leu Lys Phe Ile 225 230 235 240 Phe 63 19 PRT N-terminal of OMP-1 protein 63 Asp Pro Ala Gly Ser Gly Ile Asn Gly Asn Phe Tyr Ile Ser Gly Lys 1 5 10 15 Tyr Met Pro 64 45 DNA FECH1 64 cgggatccga attcggatgc atatcaatcg gatgcaatct ttcta 45 65 36 DNA RECH2 65 agcggccgct taagaatcac gagaactctt cgctcc 36 66 20 DNA REC1 66 acctaacttt ccttggtaag 20 

What is claimed is:
 1. An isolated polynucleotide encoding an outer membrane protein of E. canis, a variant of said outer membrane protein, or an antigenic fragment of said protein; wherein the outer membrane protein is selected from the group consisting of P30, P30a, P30-1, P30-2, P30-3, P30-4, P30-5, P30-6, P30-7, P30-8, P30-9, P30-10, P30-11, and P30-12.
 2. The isolated polynucleotide of claim 1 wherein said polynucleotide encodes an amino acid sequence which is at least 95% identical to a sequence selected from the group consisting of: amino acid 26 through amino acid 288 of the sequence, SEQ ID NO: 32, shown in FIG. 19B; amino acid 26 through amino acid 287 of the sequence, SEQ ID NO: 34, shown in FIG. 20B, amino acid 55 through amino acid 307 of the sequence, SEQ ID NO: 36, shown in FIG. 21B, amino acid 26 through amino acid 280 of the sequence, SEQ ID NO: 38, shown in FIG. 22B, amino acid 26 through amino acid 283 of the sequence, SEQ ID NO: 40, shown in FIG. 23B, amino acid 26 through amino acid 276 of the sequence, SEQ ID NO: 42, shown in FIG. 24B, amino acid 27 through amino acid 293 of the sequence, SEQ ID NO: 44, shown in FIG. 25B, amino acid 31 through amino acid 293 of the sequence, SEQ ID NO: 54, shown in FIG. 26B, amino acid 31 through amino acid 296 of the sequence, SEQ ID NO: 56, shown in FIG. 27B, amino acid 27 through amino acid 299 of the sequence, SEQ ID NO: 46, shown in FIG. 28B, amino acid 27 through amino acid 281 of the sequence, SEQ ID NO: 58, shown in FIG. 29B, amino acid 26 through amino acid 280 of the sequence, SEQ ID NO: 48, shown in FIG. 30B, amino acid 26 through amino acid 279 of the sequence, SEQ ID NO: 60, shown in FIG. 31B, amino acid 1 through amino acid 241 of the sequence, SEQ ID NO: 62, shown in FIG. 32B.
 3. The isolated polynucleotide of claim 1 wherein said polynucleotide encodes the P30 protein, a variant of the P30 protein or an antigenic fragment of said P30 protein.
 4. The isolated polynucleotide of claim 3 wherein said polynucleotide encodes a sequence which is at least 95% identical to a sequence comprising amino acid 33 through amino acid 224 of the sequence, SEQ ID NO: 32, shown in FIG. 19B.
 5. The isolated polynucleotide of claim 3 wherein said polynucleotide comprises a nucleotide sequence selected from the group consisting of the coding sequence shown in FIG. 19A, FIG. 20A, FIG. 21A, FIG. 22A, FIG. 23A, FIG. 24A, FIG. 25A, FIG. 26A, FIG. 27A, FIG. 28A, FIG. 29A, FIG. 30A, FIG. 31A, and FIG. 32B.
 6. An isolated polynucleotide encoding an outer membrane protein of E. chaffeensis, a variant of said outer membrane protein, or a an antigenic fragment of said outer membrane protein, wherein the outer membrane protein is selected from the group consisting of OMP-1, OMP-1A, OMP-1R, OMP-1S, OMP-1T, OMP-1U, OMP-1V, OMP-1W, OMP-1X, OMP-1Y, OMP-1Z, and OMP-1H.
 7. The isolated polynucleotide of claim 6 wherein the polynucleotide encodes an amino acid sequence which is at least 95% identical to a sequence selected from the group consisting of: amino acid 26 through amino acid 281 of the sequence, SEQ ID NO 2, shown in FIG. 3B; amino acid 29 through amino acid 196 of the sequence, SEQ ID NO 16, shown in FIG. 10B, amino acid 26 through amino acid 291 of the sequence, SEQ ID NO 18, shown in FIG. 11B, amino acid 1 through amino acid 131 of the sequence, SEQ ID NO 20, shown in FIG. 12B, amino acid 26 through amino acid 295 of the sequence, SEQ ID NO 22, shown in FIG. 13B, amino acid 27 through amino acid 279 of the sequence, SEQ ID NO 24, shown in FIG. 14B, amino acid 30 through amino acid 283 of the sequence, SEQ ID NO 26, shown in FIG. 15B, amino acid 25 through amino acid 275 of the sequence, SEQ ID NO 28, shown in FIG. 16B, amino acid 28 through amino acid 285 of the sequence, SEQ ID NO 30, shown in FIG. 17B, amino acid 27 through amino acid 300 of the sequence, SEQ ID NO 50, shown in FIG. 18B, amino acid 27 through amino acid 298 of the sequence, SEQ ID NO 52, shown in FIG. 33B.
 8. The isolated polynucleotide of claim 6 wherein said polynucleotide comprises a nucleotide sequence selected from the group consisting of the coding sequence set forth in FIG. 3A, FIG. 10A, FIG 11A, FIG. 12A, FIG. 13A, FIG. 14A, FIG. 15A, FIG. 16A, FIG. 17A, FIG. 18A, and FIG. 33A.
 9. An isolated polypeptide selected from the group consisting of the P30 protein, a variant of the P30 protein, an antigenic fragment of the P30 protein, the P30a protein, a variant of the P30a protein, the P30-1 protein, a variant of the p30-1 protein, the P30-2 protein, a variant of the P30-2 protein, the P30-3 protein, a variant of the P30-3 protein, the P30-4 protein, a variant of the P30-4 protein, the P30-5 protein, a variant of the P30-5 protein, the P30-6 protein, a variant of the P30-6 protein, the P30-7 protein, a variant of the P30-7 protein, the P30-8 protein, a variant of the P30-8 protein, the P30-9 protein, a variant of the P30-9 protein, the P30-10 protein, a variant of the P30-10 protein, a P30-11 protein, a variant of the P30-11 protein, the P20-12 protein, and a variant of the P30-12 protein.
 10. The isolated polypeptide of claim 9 wherein said polypeptide comprises a sequence which is at least 95% identical to a sequence selected from the group consisting of: of: amino acid 26 through amino acid 288 of the sequence, SEQ ID NO: 32, shown in FIG. 19B; amino acid 26 through amino acid 287 of the sequence, SEQ ID NO: 34, shown in FIG. 20B, amino acid 55 through amino acid 307 of the sequence, SEQ ID NO: 36, shown in FIG. 21B, amino acid 26 through amino acid 280 of the sequence, SEQ ID NO: 38, shown in FIG. 22B, amino acid 26 through amino acid 283 of the sequence, SEQ ID NO: 40, shown in FIG. 23B, amino acid 26 through amino acid 276 of the sequence, SEQ ID NO: 42, shown in FIG. 24B, amino acid 27 through amino acid 293 of the sequence, SEQ ID NO: 44, shown in FIG. 25B, amino acid 31 through amino acid 293 of the sequence, SEQ ID NO: 54, shown in FIG. 26B, amino acid 31 through amino acid 296 of the sequence, SEQ ID NO: 56, shown in FIG. 27B, amino acid 27 through amino acid 299 of the sequence, SEQ ID NO: 46, shown in FIG. 28B, amino acid 27 through amino acid 281 of the sequence, SEQ ID NO: 58, shown in FIG. 29B, amino acid 26 through amino acid 280 of the sequence, SEQ ID NO: 48, shown in FIG. 30B, amino acid 26 through amino acid 279 of the sequence, SEQ ID NO: 60, shown in FIG. 31B, amino acid 1 through amino acid 241 of the sequence, SEQ ID NO: 62, shown in FIG. 32B.
 11. The isolated polypeptide of claim 9 wherein said polypeptide is the P30 protein, a variant of the P30 protein, or an antigenic fragment of the P30 protein.
 12. The isolated polypeptide of claim 9 wherein said polypeptide comprises a sequence which is at least 95% identical to a sequence comprising amino acid 33 through amino acid 224 of the sequence, SEQ ID NO: 32, shown in FIG. 19B.
 13. An isolated polypeptide selected from the group consisting of the OMP-1 protein, the OMP-1R protein, a variant of the OMP-1R protein, the OMP-1S protein, a variant of the OMP-1S protein, the OMP-1T protein, a variant of the OMP-1T protein, the OMP-1U protein, a variant of the OMP-1U protein, the OMP-1V protein, a variant of the OMP-1V protein, the OMP-1W protein, a variant of the OMP-1W protein, the OMP-1X protein, a variant of the OMP-1X protein, the OMP-1Y protein, a variant of the OMP-1Y protein, the OMP-1Z protein, a variant of the OMP-1Z protein, the OMP-1H protein, a variant of the OMP-1H protein.
 14. The polypeptide of claim 3 wherein said polypeptide comprises a sequence which is at least 95% identical to a sequence selected from the group consisting of: amino acid 26 through amino acid 281 of the sequence, SEQ ID NO 2, shown in FIG. 3B; amino acid 29 through amino acid 196 of the sequence, SEQ ID NO 16, shown in FIG. 10B, amino acid 26 through amino acid 291 of the sequence, SEQ ID NO 18, shown in FIG. 11B, amino acid 1 through amino acid 131 of the sequence, SEQ ID NO 20, shown in FIG. 12B, amino acid 26 through amino acid 295 of the sequence, SEQ ID NO 22, shown in FIG. 13B, amino acid 27 through amino acid 279 of the sequence, SEQ ID NO 24, shown in FIG. 14B, amino acid 30 through amino acid 283 of the sequence, SEQ ID NO 26, shown in FIG. 15B, amino acid 25 through amino acid 275 of the sequence, SEQ ID NO 28, shown in FIG. 16B, amino acid 28 through amino acid 285 of the sequence, SEQ ID NO 30, shown in FIG. 17B, amino acid 27 through amino acid 300 of the sequence, SEQ ID NO 50, shown in FIG. 18B, amino acid 27 through amino acid 298 of the sequence, SEQ ID NO 52, shown in FIG. 33B.
 15. A method for diagnosing an infection with E. chaffeensis in a patient comprising the steps of: (a) providing a serum sample from the patient; (b) providing a polypeptide selected from the group consisting of the polypeptide of claim 9, the polypeptide of claim 3, and mixtures thereof; (c) contacting the serum sample with the polypeptide; and (d) assaying for the formation of a complex between antibodies in the serum sample and the polypeptide, wherein formation of said complex is indicative of infection with E. chaffeensis.
 16. The method of claim 5 wherein said polypeptide is the P30 protein, a variant of the P30 protein, or an antigenic fragment of the P30 protein.
 17. The method of claim 6 wherein the polypeptide has an amino acid sequence which is at least 95% identical to amino acid 33 through amino acid 224 of the sequence, SEQ ID NO: 32, shown in FIG. 19B.
 18. The method of claim 6 wherein said polypeptide has an amino acid sequence comprising amino acid 26 through amino acid 281 of the sequence, SEQ ID NO: 2, shown in FIG. 3B.
 19. A method for diagnosing an infection with E. canis in a Canidae patient comprising the steps of: (a) providing a serum sample from the patient; (b) providing a polypeptide of claim 9; (c) contacting the serum sample with the outer membrane protein; and (d) assaying for the formation of a complex between antibodies in the serum sample and the polypeptide, wherein formation of said complex is indicative of infection with E. canis.
 20. An antibody which binds to a protein selected from the group consisting of P30, P30a, P30-1, P30-2, P30-3, P30-4, P30-5, P30-6, P30-7, P30-8, P30-9, P30-10, P30-11, P30-12, OMP-1, OMP-1A, OMP-1R, OMP-1S, OMP-1T, OMP-1U, OMP-1V, OMP-1W, OMP-1X, OMP-1Y, OMP-1Z, OMP-1H and combinations thereof.
 21. A kit for diagnosing E. chaffeensis in a patient, said kit comprising a reagent selected from the group consisting of: the polypeptide of claim 3, the P30 protein, a variant of the P30 protein, an antigenic fragment of the P30 protein, and combinations thereof.
 22. The kit of claim 19 wherein further comprising a biomolecule for detecting interactions between the reagent and antibodies in a bodily sample of the patient.
 23. An immunogenic composition comprising a polypeptide of claim 9 or a polypeptide of claim 11 and a pharmaceutically acceptable adjuvant. 